Structural Bases of Pathogenicity and Disease


Bob (Robert) ROBINSON
Lab Location: #6-16   Email:   Tel: 65869832

Bob obtained a BSc (1987) in Chemistry from King's College, London University, an MSc (1990) in Biochemistry from University of British Columbia, and a DPhil (1996) in Structural Biology from Oxford University. During his postdoctoral studies at the Salk Institute for Biological Studies (1996-2001), Bob solved the X-ray structure of Arp2/3, an actin-nucleating complex consisting of seven proteins. In 2001, Bob was appointed as a Senior Lecturer at Uppsala University. There, the research group elucidated structures of key actin-regulating proteins. Bob became an EMBO Young Investigator in 2003. Bob joined IMCB as a Principal Investigator in 2005 and became a Research Director in 2011. He holds adjunct/affiliated positions at NTU (LKCMedicine, NISB and SBS) and at NUS (Biochemistry and SynCTI), and serves on the Editorial Boards of Open Biology and Cytoskeleton. In Singapore, the laboratory has been instrumental in deciphering the evolutionary and structural bases of how force generated from polymerizing motors is integrated into biological processes. The laboratory runs the IMCB X-ray Facility.



Structural Bases of Pathogenicity and Disease Laboratory

In plain English: The driving principle of the laboratory is that shape defines function. This laboratory uses structural biology to “see” the protein components of biological machines. Through understanding how the parts fit together, and how the components move relative to each other, we begin to understand what these biological machines do, and how and why they work. Specifically, we discover the shapes of key components of protein machines that are used by pathogens or are involved in the progression of human diseases. The laboratory is interested in all areas of aberrant protein function and misregulation, particularly in disease conditions arising from genetic mutations or external challenges, such as infection. One central theme of the laboratory is in understanding how force-generating protein machines are harnessed by biological processes, for instance during pathogen invasion.

The evolution of polymerizing protein machines. The “designs” of protein machines have been perfected (selected for) over several billion years of evolution. Through comparing the genomes from organisms that have diverged at different time points in evolution, we chart the paths of how protein machines have become more sophisticated in carrying out their functions. In this area, the laboratory has led the way in showing that the filament force generating machines from bacteria, plants and animals have followed different paths during evolution. In bacteria, there appears to be one-filament-one-function design, whereas in animals there is a universal-pool-of-actin that drives many processes.

Umesh treading the path of actin filament evolution from bacteria to animals. Read the details in Gunning et al., 2015.

Bacterial polymerizing protein machines. Many pathogenic bacteria encode their toxins and antibiotic resistance proteins on large DNA plasmids. During cell division, these plasmids need to be actively segregated to ensure the faithful inheritance of these pathogenic agents. Actin-like proteins are frequently employed as the force-generating motors used to separate pairs of plasmids prior to cell division. These proteins form filaments that elongate, which propel the plasmids attached to their tips into the daughter cells. Different plasmids have evolved varied designs of these force generating actin filaments. Presumably, they have become optimized for the size and cellular environment of each plasmid. The laboratory has made considerable progress in uncovering the unexpected and unusual designs of bacterial motor proteins. Two of the most significant discoveries are the actin (ParM) proteins from Bacillus thuringiensis (Jiang et al, 2016) and Clostridium tetani (Popp et al., 2012), which form remarkable antiparallel nanotubules and twisted filaments, respectively.

David and Shimin discover a novel actin motor from Bacillus thuringiensis that forms nanotubules. Read their findings in Jiang et al, 2016.

The universal-pool-of-actin in eukaryotes. Animals have adopted a universal-pool-of-actin to power movement in a vast range of biological processes, such as cell locomotion and phagocytosis. Thus, they use a common molecular machine to power many types of biological movement. The universal-pool-of-actin strategy requires the actin polymerization machine to be highly regulated to ensure that the actin pool is always maintained, no matter the demands of any single process. The laboratory has made significant discoveries in determining how the pool of actin monomers is maintained in an elevated state, how filament lengths are regulated by capping proteins, and how the force from actin polymerization is integrated into specific processes.

Albert conquers the structure of thymosin-β4 (rainbow) bound to an actin monomer (black/white). Read how this complex maintains the pool of actin monomers in Xue et al., 2014.

Subversion of human actin by pathogens. Since the actin filament has barely changed in the one billion years that separate humans and yeast, many pathogens have evolved to exploit or disable this force-generating machine. One such example is the bacterium Yersinia pestis, the cause of the bubonic plague, which has had a profound affect on the course of human civilization during outbreaks known as the Plague of Justinian and the Black Death. The laboratory has made a major advance in understanding how this pathogen evades the human immune system. From determining the shape of a complex between a protein from the pathogen (YopO) and actin, the laboratory has uncovered how this organism can turn off the process of phagocytosis, which otherwise would destroy the pathogen. The laboratory has an active program in studying other host-pathogen interactions.

Wei Lin contemplates how the Black Death agent, Yersinia pestis (pink), uses YopO (black) to disable actin (cyan) polymerization and turn off phagocytosis. Read her thoughts in Lee et al. 2015.

Exploiting our discoveries. Discoveries in basic science can occasionally be repurposed by humans to create new tools, reagents and potential drugs in a similar way that pathogens have hijacked the actin force-generating system (previous section). One such discovery comes from collaboration with the Manser laboratory, in which an artificial protein construct (iBox:PAK4) spontaneously forms crystals when expressed within mammalian cells. The quality of these crystals was sufficient to solve the structure inside an intact cell, from which we realized that it would be possible to include other proteins into the crystal scaffold created by iBox:PAK4. We are developing this in cellulo crystal system for many potential applications, such as cellular sensors, probes, drug:ligand interactions, drug development, and as a protein expression and purification matrix.

Read how he solved the structure within intact cells in” with “Read how he solved the structure of the iBox:PAK4 scaffold within intact cells in Baskaran et al. 2015.

A GFP hybrid crystal growing inside a living cell.

Techniques The laboratory specializes in a range of structural biology and biophysical techniques, which include: protein crystallography, electron microscopy, total internal reflection fluorescence (TIRF) microscopy, small angle X-ray scattering (SAXS), fluorescence, dynamic light scattering and mass spectrometry (in collaboration with Gunaratne and Sobota groups). These methods allow the determination of the conformations and dynamics of protein complexes and interactions, which provide understanding of how each protein performs, or fails to perform, in its biological function. We are also actively engaged in drug design and involved in structural biology method development.
The laboratory uses several synchrotron facilities including: Diamond, NSRRC, ESRF and ALS.

Collaborations, Students and Postdocs The laboratory collaborates extensively within Singapore and internationally. Singapore connections include joint projects with the A*STAR entities BioTrans, BII, ICES, and the p53lab, and with SynCTI, NUS and NTU, often supplementing programs within these organizations with structural biology expertise. The laboratory is keen to expand this portfolio particularly in establishing links with industry and clinical researchers. Similarly, we encourage applications from A*STAR scholars, returning scholars and prospective scholars, as well as from potential graduate students and postdocs that are either self-financed or willing and eligible to apply for one of the following schemes:




NTU Institute Structural Biology


Many thanks to Ciccy Wang and Ace Khong for help with the images and web pages.


Department: Robert ROBINSON

Name: Clement Pierre Marcel SCIPION

Designation: SINGA Student


Name: Dennis Mweti MWANGANGI

Designation: SINGA Student


Name: Habiba ZORGATI

Designation: Research Fellow


Name: Caner AKIL

Designation: SINGA Student


Name: Samson ALI

Designation: SINGA Student



Brichkina, A., Nguyen, T. M. N., Baskar, R., Wee, S., Gunaratne, J., Robinson, R. C. & Bulavin, D. V.
Proline isomerisation as a novel regulatory mechanism for p38MAPK activation and functions.
Cell Death Differ. (2016) In press.

Jiang, S., Narita, A., Popp, D., Ghoshdastider, U., Lee, L. J., Srinivasan, R., Mohan K. Balasubramanian, M. K., Oda, T., Koh, F., Larsson, M., & Robinson, R. C.
Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.
Proc. Natl. Acad. Sci. U.S.A. (2016) 113, E1200-1205.

Baskaran, Y., Ang, K. C., Anekal, P. V., Chan, W. L., Grimes, J. M., Manser, E., & Robinson, R. C.
An in cellulo derived structure of PAK4 in complex with its inhibitor Inka1.
Nat. Commun. (2015) 6, 8681.

Chumnarnsilpa, S., Robinson, R. C., Grimes, J. M., & Leyrat, C.
Calcium-controlled conformational choreography in the N-terminal half of adseverin.
Nat. Commun. (2015) 6, 8254.

Ghoshdastider, U., Jiang, S. M., Popp, D. & Robinson, R. C.
In search of the primordial actin filament.
Proc. Natl. Acad. Sci. U.S.A. (2015) 112, 9150-9151.

Tankrathok, A., T., Iglesias-Fernández, J., Williams, R., Pengthaisong, S., Baiya, S., Hakki, Z., Robinson, R, C., Hrmova, M., Rovira, C., Williams, S. & Ketudat Cairns, J.
 A single glycosidase different pyranoside ring transition state conformations for hydrolysis of mannosides and glucosides.
ACS Catal. (2015) 5, 6041–6051.

Go, M., Wongsantichon. J., Cheung, V. W. N., Chow, J, Y., Robinson, R. C.* & Yew, W. S.
Synthetic Polyketide Enzymology: A Platform for Biosynthesis of Anti-Microbial Polyketides.
ACS Catal. (2015) 5, 4033-4042.

Gunning, P., Ghoshdastider, U., Whitaker, S., Popp, D. & Robinson, R. C.
 The evolution of compositionally and functionally distinct actin filaments.
J. Cell Sci. (2015) 128, 2009-2019.

Lee, W. L., Grimes, J. M. & Robinson, R. C.
Yersinia effector YopO utilizes actin as bait to phosphorylate proteins that regulate actin polymerization.
Nat. Struct. Mol. Biol.  (2015) 22, 248-255.

Van Overbeke, W., Wongsantichon, J., Everaert, I., Verhelle, A., Zwaenepoel, O., Loonchanta, A., Burtnick, L. D., De Ganck, A., Hochepied, T., Haigh, J., Cuvelier, C., Derave, W., Robinson, R. C.* & Gettemans, J.
An ER-directed gelsolin nanobody establishes therapeutic merit in the gelsolin amyloidosis mouse model by shielding mutant plasma gelsolin from furin proteolysis.
Hum. Mol. Genet. (2015) 24, 2492-2450.

Ranok, A., Wongsantichon, J., Robinson, R. C.* and Suginta, W.
Structural and thermodynamic insights into chitooligosaccharide binding to human cartilage chitinase 3-like protein 2 (CHI3L2 or YKL-39).
J. Biol. Chem. (2015) 290, 2617-2629.

Vu, T. T., Koo, B. K., Song, J. A., Chong, S. H., Park, C. R., Nguyen, M. T., Jeong, B., Ryu, H. B., Seong, J. Y., Jang, Y. J., Robinson, R. C. & Choe, H.
Soluble overexpression and purification of bioactive human CCL2 in E. coli by maltose-binding protein.
Mol. Biol. Rep. (2015) 42, 651-663.

Xue, B., Leyrat, C., Grimes, J. M. & Robinson, R. C.
The structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.
 Proc. Natl. Acad. Sci. U.S.A. (2014) 111, E4596-605.

Lv, C., Gao, X., Li, W., Xue, B., Qin, M., Burtnick, L. D., Zhou, H., Cao, Y., Robinson, R. C.* & Wang, W.
Single molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.
 Nat. Commun. (2014) 5, 4623.

Cheung, V. W., Xue, B., Hernandez-Valladares, M., Go, M. K., Tung, A., Aguda, A. H., Robinson, R. C.* & Yew, W. S.
Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis.
PLoS ONE (2014) 9, e103598.

Yang, W., Thein, S., Lim, C.-Y., Ericksen, R. E., Sugii, S., Xu, F., Robinson, R. C., Kim, J. B. & Han, W.
Arp2/3 complex regulates adipogenesis by controlling cortical actin remodelling.
Biochem. J. (2014) 464, 179-192.

Chee, S., Wongsantichon, J., Tng, Q. S., Robinson, R. C., Verma, C., Lane, D. P., Brown, C. J., & Ghadessy, F. J.
Structure of a stapled peptide antagonist bound to nutlin-resistant Mdm2.
PLoS ONE (2014) 9, e104914.

Smadbeck, J., Chan, K. H., Khoury, G. A., Xue, B., Robinson, R. C., Hauser, C. A. & Floudas, C. A. De novo design and experimental characterization of ultrashort self-associating peptides.
PLoS Comput. Biol. (2014) 10, e1003718.

Vu, T. T., Jeong, B., Yu, J., Koo, B. K., Jo, S. H., Robinson, R. C. & Choe H.
Soluble prokaryotic expression and purification of crotamine using an N-terminal maltose-binding protein tag.
Toxicon (2014) 92, 157-165.

Jeong, T. H., Son, Y. J., Ryu, H. B., Koo, B. K., Jeong, S. M., Hoang, P., Do, B. H., Song, J. A., Chong, S. H., Robinson, R. C. & Choe, H.
Soluble expression and partial purification of recombinant human erythropoietin from E. coli.
Protein Expr. Purif. (2014) 95, 211-218.

Xue, B., Chow. J. Y., Baldansuren, A., Yap, L. L., Gan, Y. H., Dikanov, S. A., Robinson, R. C.* & Yew, W. S. Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase.
Biochemistry (2013) 52, 2359-2370.

Subramanian, D., Huang, J., Sevugan, M., Robinson, R. C., Balasubramanian, M. K. & Tang, X. Insight into actin organization and function in cytokinesis from analysis of fission yeast mutants.
Genetics (2013) 194, 435-446.

Dudgeon, C., Shreeram, S., Tanoue, K., Mazur, S. J., Sayadi, A., Robinson, R. C., Appella, E. & Bulavin, D. V.
Genetic variants and mutations of PPM1D control the response to DNA damage.
 Cell Cycle (2013) 12, 2656-2664.

Tankrathok, A., Iglesias-Fernández, J., Luang, S., Robinson, R. C., Kimura, A., Rovira, C., Hrmova, M., & Ketudat Cairns,
J. Structural analysis and insights into glycon specificity of the rice GH1 Os7BGlu26 β-D-mannosidase.
Acta Cryst. (2013) D69, 2124-2135.

Song, J.-A., Koo, B.-K., Chong, S.-H., Kim, K., Choi, D. K., Vu1, T. T. T., Nguyen, M. T., Jeong, B., Ryu, H.-B., Kim, I., Jang, Y. J., Robinson, R. C. & Choe, H.
Soluble expression of human leukemia inhibitory factor in Escherichia coli and its simple purification.
 PLoS ONE (2013) 12, e83781.

Xue, B. & Robinson, R. C.
Guardians of the actin monomer.
Eur. J. Cell Biol. (2013) 92, 316-332.

Ghoshdastider, U., Popp, D., Burtnick, L. D., & Robinson, R. C.
The expanding superfamily of gelsolin homology domain proteins.
Cytoskeleton (2013) 70, 775-795.

Nag, S., Larsson, M., Robinson, R. C.* & Burtnick, L. D.
Gelsolin: The tail of a molecular gymnast.
Cytoskeleton (2013) 70, 360-84.

Popp, D., Narita, A., Lee, L. J., Larsson, M. & Robinson, R. C.
Microtubule-like properties of the bacterial actin homolog ParM-R1.
J. Biol. Chem. (2012) 287, 37078-37088.

Popp, D., Narita, A., Lee, L. J., Ghoshdastider, U., Xue, B., Srinivasan, R., Balasubramanian, M. K., Tanaka, T. & Robinson, R. C.
A novel actin-like filament structure from Clostridium tetani.
J. Biol. Chem. (2012) 287, 21121-21129.

Popp, D. & Robinson, R.C.
Supramolecular cellular filament systems: How and why do they form?
Cytoskeleton (2012) 69, 71-87.

Lukman, S, Robinson, R. C., Wales, D. & Verma, C. S.
Conformational dynamics of capping protein and interaction partners: Simulation studies.
Proteins (2012) 80, 1066-1077.

Wongsantichon, J., Robinson, R. C. & Ketterman, A.
Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding.
Arch. Biochem. Biophys. (2012) 521, 77-83.

Rajakannan, V., Lee, H-S., Chong, S-H., Ryu, H-B., Bae, J-Y., Whang, E-Y., Huh, J-W, Cho, S-W., Kang, L-W., Choe, H. & Robinson, R. C.
Structural basis of cooperativity in human UDP-glucose dehydrogenase.
PLoS ONE (2011) 6, e25226.

Chuenchor, W., Pengthaisong, S., Robinson, R. C., Yuvaniyama, J., Svasti, J. & Cairns, J. R.
The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase.
J. Struct. Biol. (2011) 173, 169-179.

Popp, D. & Robinson, R. C.
Many ways to build an actin filament.
Mol. Microbiol. (2011) 80, 300-308.

Popp, D., Narita, A., Maeda, K., Fujisawa, T., Ghoshdastider, U., Iwasa, M., Maeda, Y. & Robinson, R. C.
Filament structure, organization, and dynamics in MreB sheets.
J. Biol. Chem. (2010) 285, 15858-15865.

Hernandez-Valladares, M., Kim, T., Kannan, B., Tung, A., Aguda, A. H., Larsson, M, Cooper, J. A. & Robinson, R. C.
Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.
Nat. Struct. Mol. Biol. (2010) 17, 497-503.

Popp, D., Xu, W., Narita, A., Brzoska, A. J., Skurray, R. A., Firth, N., Goshdastider, U., Maeda, Y., Robinson, R. C. & Schumacher, M. A.
Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation.
J. Biol. Chem. (2010) 285, 10130-10140.

Wang, H., Robinson, R. C.* & Burtnick, L. D.
The structure of native G-actin.
Cytoskeleton (2010) 7, 456-465.

Popp, D., Iwasa, M., Erickson, H. P., Narita, A., Maeda, Y. & Robinson, R. C.
Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.
J. Biol. Chem. (2010) 285, 11281-11289.

Chow, J.Y., Xue, B., Lee, K. H., Tung, A., Wu, L., Robinson, R. C.* & Yew, W. S.
Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily.
J. Biol. Chem. (2010) 285, 40911-40920.

Wongsantichon, J., Robinson, R. C. & Ketterman, A. J.
Structural contributions of a delta class glutathione transferase active site residues to catalysis.
 Biochem. J. (2010) 428, 25-32.

Popp, D., Narita, A., Ghoshdastider, U., Maeda, K., Maeda, Y., Oda, T., Fujisawa, T., Onishi, H., Ito, K. & Robinson, R. C.
Polymeric structures and dynamic properties of the bacterial actin AlfA.
J.Mol. Biol. (2010) 397, 1031-1041.

Popp, D., Narita, A., Iwasa, M., Maeda, Y. & Robinson, R. C.
Molecular mechanism of bundle formation by the bacterial actin ParM.
Biochem. Biophys. Res. Commun. (2010) 391, 1598-1603.

Popp, D. & Robinson, R. C.
The suprastructures of the bacterial cytoskeleton and their physical origin.
Commun. Integr. Biol. (2010) 3, 451-453.

Chumnarnsilpa, S., Lee, W. L., Nag, S., Kannan, B., Larsson, M., Burtnick, L. D. & Robinson, R. C. The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.
Proc. Natl. Acad. Sci. U.S.A. (2009) 106, 13719-13724.

Nag, S., Ma, Q., Wang, H., Chumnarnsilpa, S., Lee, W. L., Larsson, M., Kannan, B., Hernandez-Valladares, M., Burtnick, L. D. & Robinson, R. C.
Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.
Proc. Natl. Acad. Sci. U.S.A. (2009) 106, 13719-13724.

Wang, H., Chumnarnsilpa, S., Loonchanta, A., Li, Q., Kuan, Y. M., Robine, S., Larsson, M., Mihalek, I., Burtnick, L. D. & Robinson, R. C.
Helix-straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins.
 J. Biol. Chem. (2009) 284, 21265-21269.

Siritapetawee, J., Thammasirirak, S., Robinson, R. C. & Yuvaniyama, J.
The 1.9 Å X-ray structure of egg-white lysozyme from Taiwanese soft-shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences from the standard chicken-type lysozyme.
J. Biochem. (2009) 145, 193-198.

Songsiriritthigul, C., Pantoom, S., Aguda, A. H., Robinson, R. C. & Suginta, W.
Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism.
J. Struct. Biol. (2008) 162, 1-9.

Chuenchor, W., Pengthaisong, S., Robinson, R. C., Yuvaniyama, J. Oonanant, W., Bevan, D. R., Esen, A., Chen, C. J., Opassiri, R., Svasti, J. & Cairns, J. R.
Structural insights into rice BGlu1 beta-glucosidase oligosaccharide hydrolysis and transglycosylation.
J. Mol. Biol. (2008) 277, 1200-1215.

Burtnick, L. D. & Robinson, R. C.
Gelsolin and disease.
Protein reviews: Actin binding proteins and disease. Springer. (2008) 8, 188-199.

Zaccai, N. R., May, A. P, Robinson, R. C., Burtnick, L. D., Crocker, P. R., Brossmer, R., Kelm, S. & Jones, E. Y.
Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin.
J. Mol. Biol. (2007) 365, 1469-1479.

Aguda, A. H., Sakwe, A. M., Rask, L. & Robinson, R. C.
Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16. Acta Cryst. (2007) F63, 291-293.

Xue, B., Aguda, A. H. & Robinson, R. C.
Models of actin-bound forms of the beta-thymosins.
Ann. N. Y. Acad. Sci. (2007) 12, 56-66.

Huh, J. W., Robinson, R. C., Lee, H. S., Lee, J. I., Heo, Y. S., Kim, H. T., Lee, H. J., Cho, S. W. & Choe, H.
Expression, purification, crystallization, and preliminary X-ray analysis of the human UDP-glucose dehydrogenase.
Protein Pept. Lett. (2006) 13, 859-862.

Aguda, A. H., Xue, B., Irobi, E., Preat, T. & Robinson, R. C.
The structural basis of actin interaction with multiple WH2 motif-containing proteins.
Structure. (2006) 14, 469-476.

Chumnarnsilpa, S., Loonchanta, A., Xue, B., Choe, H., Urosev, D., Wang, H., Lindberg, U., Burtnick, L. D., & Robinson, R. C.
Calcium ion exchange in crystalline gelsolin.
J. Mol. Biol. (2006) 357, 773-783

Urosev, D., Ma, Q., Tan, A. L. C., Robinson, R. C. & Burtnick, L. D.
The structure of gelsolin bound to ATP.
J. Mol. Biol. (2006) 357, 765-772.

Lee, H. S., Robinson, R. C., Joo, C. H., Lee, H., Kim, Y. K. & Choe, H.
Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin.
Biochem. Biophys. Res. Commun. (2006) 342, 702-709.

Songsiriritthigul, C., Yuvaniyama, J., Robinson, R. C., Vongsuwan, A., Prinz, H. & Suginta, W. Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae.
Acta Cryst. (2005) F61, 895-898.

Huang, S., Robinson, R. C., Gao, L. Y., Matsumoto, T., Brunet, A., Blanchoin, L. & Staiger, C. J. Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.
Plant Cell
(2005) 17, 486-501.

Irobi, E., Aguda, A. H., Larsson, M., Guerin, C., Yin, H. L., Burtnick, L. D., Blanchoin, L. & Robinson, R. C.
Structural basis of actin sequestration by thymosin-b4: Implications for WH2 proteins.
EMBO J. (2004) 23, 3599-3608.

Burtnick, L. D., Urosev, D., Irobi, E., Narayan, K. & Robinson, R. C.
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.
EMBO J. (2004) 23, 2713-272.

Irobi, E., Burtnick, L. D., Urosev, D., Narayan, K. & Robinson, R. C.
From the first to the second domain of gelsolin: a common path on the surface of actin?
FEBS Lett. (2003)552, 86-90.

Narayan, K., Chumnamsilpa, S., Choe, H., Irobi, E., Urosev, D., Lindberg, U., Schutt, C. E., Burtnick, L. D. & Robinson, R. C.
Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin.
FEBS Lett. (2003) 552, 82-85.

Larsson, M., Hjälm, G., Sakwe, A. M., Engström, Å., Höglund, A. S., Larsson, E. Robinson, R. C., Sundberg, C. & Rask, L.
Selective interaction of megalin with PSD-95-like MAGUK proteins. Biochem. J. (2003) 373, 381-391.

Choe, H., Burtnick, L. D., Mejillano, M., Yin, H. L., Robinson, R. C.* & Choe, S.
The calcium activation of gelsolin: Insights from the 3.0 Å structure of the G4-G6/actin complex.
 J. Mol. Biol. (2002) 324, 691-702.

Robinson, R. C., Turbedsky, K., Kaiser, D. A., Higgs, H., Marchand, J.-B.  Choe, S. & Pollard, T. D. Crystal Structure of Arp2/3 Complex.
Science. (2001) 294, 1679-1684. Highlighted by Faculty 1000 Biology.

Robinson, R. C., Choe, S., & Burtnick, L. D.
The disintegration of a molecule: The role of gelsolin in FAF, familial amyloidosis (Finnish type).
Proc. Natl. Acad. Sci. U.S.A. (2001) 98, 2117-2118.

Robinson, R. C., Choe, S. & Burtnick, L. D.
Structure and function of gelsolin. Molecular interactions of Actin: Actin structure and actin-binding proteins.
Results Probl. Cell Differ. (2001) 32, 201-211.

Blanchoin, L., Robinson, R. C., Choe, S. & Pollard, T. D.
Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure.
J. Biol. Chem. (2000) 295, 203-211.

Robinson, R. C., Mejillano, M., Le, V. P., Burtnick, L. D., Yin, H. L. & Choe, S.
Domain movement in a gelsolin activation switch.
Science (1999) 286,1939-1942.

Robinson, R. C., Radziejewski, C., Spraggon, G., Greenwald, J., Kostura, M., Burtnick, L. D., Stuart, D. I., Choe, S. & Jones, E. Y.
The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site.
Prot. Sci. (1999) 8, 2589-2597.

May, A. P., Robinson, R. C., Aplin, R. T., Bradfield, P., Crocker, P. R. & Jones, E. Y.
The structure of a sialic acid binding fragment of sialoadhesin in the presence of ligand.
Mol. Cell  (1998) 1, 719-728.

Choe, S. & Robinson, R. C.
An ingenious filter: the structural basis for ion channel selectivity.
Neuron (1998) 20, 821-823.

Burtnick, L. D., Koepf, E. K., Grimes, J., Jones, E. Y., Stuart, D. I., McLaughlin, P. J. & Robinson, R. C.
The crystal structure of plasma gelsolin: Implications for actin severing, capping and nucleation.
(1997) 90, 661-670.

May, A. P., Robinson, R. C., Aplin, R. T., Bradfield, P., Crocker, P. R. & Jones, E. Y.
Expression, crystallization and preliminary X-ray analysis of a sialic acid binding fragment of sialoadhesin in the presence of ligand.
Prot. Sci. (1997) 6, 717-721.

Robinson, R. C., Radziejewski, C., Stuart, D. I. & Jones, E. Y.
Crystals of the neurotrophins.
Prot. Sci. (1996) 5, 973-977.

Jones, E. Y., Harlos, K., Bottomley, M. J., Robinson, R. C., Driscoll, P. C., Edwards, J. M., Clements, J. M., Dudgeon, T. J. & Stuart, D. I.
Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule 1 at 1.8 Å resolution.
Nature (1995) 373, 539-544.

Robinson, R. C., Radziejewski, C., Stuart, D. I. & Jones, E. Y.
The structure of the brain derived neurotrophic factor/neurotrophin 3 heterodimer.
Biochemistry (1995) 34, 4139-4146.

Robinson, R. C., Grey, L. M., Staunton, D., Stuart, D. I., Heath, J. K. & Jones, E. Y. The structure of murine leukaemia factor.
Ann. New York Acad. Sci.
(1995) 762, 179-189.

Robinson, R. C., Grey, L. M., Staunton, D., Vankelecom, H., Vernallis, A. B., Moreau, J-F., Stuart, D. I., Heath, J. K. & Jones, E. Y.
The crystal structure and biological function of leukaemia inhibitory factor: Implications for receptor binding.
Cell (1994) 77, 1101-1116.

Bottomley, M. J., Robinson, R. C., Driscoll, P. C., Harlos, K., Stuart, D. I., Aplin, R. T., Clements, J. M., Jones, E. Y. & Dudgeon, T. J.
Crystallization and preliminary X-ray diffraction characterization of both a native and selenomethionyl VLA-4 binding fragment of VCAM-1.
J. Mol. Biol. (1994) 244, 464-468.

Radziejewski, C. & Robinson, R. C.
Heterodimers of the neurotrophic factors: Formation, isolation and differential stability.
Biochemistry (1993) 32, 13350-13356.

Radziejewski, C., Robinson, R. C., DiStefano, P. S. & Taylor, J. W.
Dimeric structure and conformational stability of BDNF and NT-3.
Biochemistry (1992) 31, 4431-4436.

Robinson, R. C. & Burtnick, L. D.
The stabilization of horse vitamin D binding protein by disulphide bonds.
Biochem. Cell Biol. (1992) 70, 10-15.

* Indicates corresponding author where not last author


Book Chapters

Burtnick, L. D. & Robinson, R. C.
Gelsolin and disease.
Protein reviews: Actin binding proteins and disease. Springer. (2008) 8, 188-199.

Xue, B., Aguda, A. H. & Robinson, R. C.
Models of actin-bound forms of the beta-thymosins.
Ann. N. Y. Acad. Sci.
(2007) 12, 56-66.

Robinson, R. C., Choe, S. & Burtnick, L. D.
Structure and function of gelsolin. Molecular interactions of Actin: Actin structure and actin-binding proteins.
Results Probl. Cell Differ. (2001) 32, 201-211.

Robinson, R. C., Grey, L. M., Staunton, D., Stuart, D. I., Heath, J. K. & Jones, E. Y.
The structure of murine leukaemia factor.
Ann. New York Acad. Sci. (1995) 762, 179-189.

Meet the Lab

Meet the Lab

BR Lab Photos

Tropical BR Lab Christmas Party – Dec. 2015

Typical BR Lab Meeting – Dec. 2015

Pursuing the perfect Pla Pao - Golden Mile - Summer 2014

Leaving no leaf unturned - Samy's - summer 2013

Research Scientists


Candied Chinese hawthorns on a bamboo skewer are my favorite, as the sweet and sour taste always gives me a good appetite.  The projects I get from the lab are quite tasty too, so I can’t help taking them one after another.  And that’s why I’ve been here for so many years...


David POPP

David started his quest to understand the cells physiologically relevant biological filament systems and the search for Nature’s primordial actin- and microtubule-like filaments over 30 years ago at the MPI for Medical Research in Heidelberg where he solved the structure of one of Nature’s most abundant filaments, F-actin together with Ken Holmes. He has worked at Brandeis University with Hugh Huxley on muscle acto-myosin filament contraction using electron microscopy and at Spring8, Japan with Yuichiro Maeda on bacterial filament systems, before joining IMCB in 2009. His main drive at present is to solve structures of DNA segregating polymers by cryo-electron microscopy and to use these systems as biological nano-machines and nano-wires.

In his spare time, David is a fly fisherman, fly tier, fly caster and bamboo fly rod maker. His next destination: Jurassic lake, Patagonia


Postdoctoral Fellows


Hi I’m Shimin!
I was very happy and lucky to join Bob’s lab at August, 2011. Here, I focus on the bacterial filament systems with Dr David. These filament systems play a key role in the life cycle of bacteria, including many pathogenic bacteria. Although there’s still a long, long way to go, our final target is to uncover the mechanism of filament systems and find new antibiotics targeting these systems.  After working, I like cooking, eating, drinking, watching movie, cycling and playing badminton. Anyway, I am very enjoying my studies and research in this fantastic team.


Wei Lin LEE

As the adage goes - choose a job you love, and you will never have to work a day in your life. This pretty much sums up life in BR lab for me. I did my undergraduate in National University of Singapore; and with a scholarship from A*STAR I did my D.Phil at Oxford University. During my DPhil, I was intrigued by how a great number of disease-causing bacteria have evolved mechanisms to manipulate the human actin cytoskeleton for survival. So I embarked on studying how Yersinia pestis, one of the deadliest bacteria in human history, perturbs the host actin cytoskeleton to disrupt the process in which host immune cells take up and destroy pathogens. Following on this work, I currently study other disease-causing bacteria to unravel their arsenal of weaponry against the host actin cytoskeleton, and to find alternative methods for treatment of the diseases they cause. When I am not working, I spend time with my daughter who just turned 1 year old! I enjoy travelling, reading and watching science-fiction action-horror films.



Jantana's here. Being part of BR lab has given me a great opportunity to do protein structural studies (X-ray crystallography and electron microscopy) and to understand protein (actin and its playmates) dynamics. Outside our working space, I also enjoy a drink or two and sometimes have good badminton challenges with the lab crew.


Research Officer

Holiday in Hakone


I joined BR group in 2010 as a research officer. Prior to that, I worked in a few institutions, including Gene Lab Diagnostic, IMA and GIS A*STAR. I received my BSc in Biology and MSc in Immunology. After work, I enjoy spending time with my family and friends. I also enjoy cooking and traveling.


Graduate Students


Hi I’m Clément!
Before joining the lab, I performed my previous studies in the French ‘Grande école’ école Centrale de Marseille, where I obtained my B. Eng. and M. Eng. Here, my research focuses on actin severing and sequestering peptides that I try to characterize and optimize, in order to understand the mechanisms of these processes.

In my spare time, I enjoy reading, playing badminton, running, listening to Classic Rock and an occasional Blonde Ale. When not organizing a Lab barbecue party to gather former and new lab members and their families together, I love traveling and meeting new people from all over the world. Working in Singapore and especially in Bob’s lab allows me to fulfill this aspiration on a daily basis!


Lin Jie LEE

Hi, I’m Lin Jie. I am a AGS (local) phd student and I have been in BR lab since 2009. I am attached to Laurent Blanchoin's lab in France till Sept, I am doing work on the TIRF microscopy and glass surface micro-patterning techniques there. I will be back!


Eleanor MARTIN

Hi I’m Ellie. I’ve recently joined the group as part of my PhD at the University of Manchester. My research focuses on studying the interaction between the actin cytoskeleton and the chloride ion channel implicated in cystic fibrosis – CFTR.

Before joining the lab, I studied at the University of Bath, and also spent some time studying Mandarin Chinese in Taiwan. In my spare time I enjoy trying to keep up my study of the language, as well as running, cooking, and travelling.


Samson ALI

I graduated from the University of Ghana with a BSc (Biochemistry) degree and proceeded to attaining an MSc (Infection and Immunity) from the University of Leeds, UK. Currently pursuing a PhD in the National University of Singapore  and working on characterization of plasmid segregation systems in Prof. Robert Robinson’s Lab.

My leisure is filled with travelling, sightseeing, playing soccer and listening to good music. With determination and in the right lab with necessary expertise as Bob’s, I believe any academic height is attainable!


Caner AKIL

Hi, I am Caner,
I obtained my BSc (2011) from University of Caucasian, my MSc (2014) from Izmir Institute of Technology in Turkey. I joined Bob’s laboratory (2015) to elucidate structure and biochemical properties of gelsolin-like and actin-like proteins in different livings.

My favorite acts are riding motorcycles for long distance travel and listening authentic Anatolia music.



Working on proteins that come at the extreme end of the central dogma is quite interesting, you get go through all the processes including DNA replication, transcription before you get to your final destination which is translation albeit before post translational modifications.  Working in the BR lab under the mentorship of Prof Robinson has helped me acquire a wealth of knowledge in structural biology.

With a BSc. in Biomedical Sciences and MSc in Structural Molecular Biology this opportunity has availed me a chance to bridge into the realm of deeper science. I am glad to be part of one of the best laboratories in the world and under the mentorship of the coolest boss ever. Join me in my free time as I visit art enclaves the world has to offer.


Undergraduate Students


Hi I’m Ha Lam!
I am currently an undergraduate, pursuing a degree in Biological Sciences at Nanyang Technological University (NTU). I joined Dr. Robinson’s Lab to understand what the research world entails and also to develop my research interests. Currently, my project here concerns actin interacting protein 1 (aip1).

class="bodyfontlabs" align="justify">I like taking slow walks, reading, solving puzzles and playing the piano in my free time. I love exploring, learning from the seniors as well as interacting with people. Therefore, I really enjoy and treasure my time in Dr. Robinson’s lab.



Jennifer LUU (2016)

A native of Vancouver, Canada, where she is completing her BSc at the University of British Columbia, Jennifer was a SIPGA intern in Bob’s lab. Her project focused on determining the relationship of the Rab GTPases with the anti-oncogenic drug Apratoxin, in hopes of identifying it as a drug target.  When not singing a love song to convince her bacteria to behave nicely, Jennifer enjoys drawing, running, hiking (she briefly rolled down a mountain once), or having a good time with friends – sometimes with a beer in hand..


Ciccy WANG (2015)

Hi, I'm Ciccy. I'm currently studying B. Science Adv at the University of Sydney. I came to Bob's lab as a 2 month SIPGA student in my summer holidays to get some research experience. I did a project with Jantana where I attempted to purify and crystallise hot worm actin-binding proteins to determine their structure. I really enjoyed it despite the bacteria being very temperamental with protein expression. I really like travelling so I always try and participate in science projects overseas. In my spare time, I enjoy drawing, reading and gaming (Nintendo DS series). Thanks to the lab for taking me on and helping me!


Pavithra SINGARAVELU (2015)

Hello, I am Pavithra SINGARAVELU from India. People call me 'Pavi', Easy right? I was a NUS scholar from the Dept. of Biological Sciences (DBS), NUS and I worked in collaboration with Bob's lab for my PhD. I recently graduated in 2015 and now hold a CNRS post-doc position at CEA, Grenoble. I learnt a lot from Bob and other BRians, that has moulded me as a good researcher. Working with BR group was fun and fabulous. I miss everyone and will cherish BR group memories forever.


Liling WU (2015)

I am Liling and I just graduated this year. I was working in both Ernesto’s and Bob’s labs studying protein methyltransferases over the past four years. It was such a special experience to study and live in Singapore.


Widyawillis SELAMAT (2015)

Bob was on my thesis advisory committee when I was pursuing my doctorate, and I was always intrigued by his different hairstyles/looks and intelligence each time there was at a meeting. Anyway, I decided to serve my bond with A*STAR from 2012-2015 in his lab because I believed there was plenty that I could learn, and I was not disappointed.  I worked mainly on the actin-binding protein profilin and SILAC-coupled affinity purifications became my forte.

Led by the kindest and most amazing boss ever (no joke!), the BR group was truly fantastic and made science extremely enjoyable. An especially memorable experience indeed, as I ended my stint there with a beautiful addition to my family. Thank you for such great memories!In my free time, I like to travel, running, swimming, listen to calm music and spend my time with my beautiful aquarium.


Balakrishnan KANNAN (2014)

After spending wonderful time in Bob’s lab working on actin-binding proteins, I am now playing with optics and fluorescence! It is awesome to see objects under the different microscopes – with different colours (they are false anyway!) – and all the different interactions!


David Szatmar (2014)

Hi! I am Dávid (or Daavid)

I was a PhD student in Hungary, Medical School of Pécs, Dept. of Biophysics. Then I spent two fantastic years in Bob's Lab thanks to A*STAR, Research Attachment Program where I got a high level Asian and scientific experience. There I was focused on the dynamical structure of gelsolin. Recently, I returned back to Hungary and we have a collaboration project about MreB characterization. I am glad and my pleasure to know this amazing team of BRers.


Yong Zi TAN(2014)

Hello, I am Yong Zi! I was a research officer in Bob's lab for a year, working under Jantana to crystallise a series of actin-binding proteins and complexes. I learnt a lot in the lab, and have a lot of fun too! I have continued with my passion for structural biology, and I am now doing my PhD at Columbia University doing single particle electron microscopy.


Wee Lee CHAN (2014)

Hi, I'm Wee Lee. I was a post-doc in the Robinson lab from January to July 2014 where I worked on Bob's project to understand the structure and function of serine/threonine protein kinase 4 (PAK4).  I also served a secondary function in the lab as Bob's occasional crossword partner. Prior to joining the lab, I went up to St Edmund Hall, Oxford in 2004 to read Biochemistry, after which I did a PhD under Randy Read's supervision at Cambridge.
I am now working on my medical degree at Duke-NUS Medical School, with the hope of becoming a physician-scientist at some point in the distant future. I used to spend my spare time hillwalking, sailing and playing rugby. I also enjoy reading, particularly Graham Greene and Evelyn Waugh.  These days,however, I am happy just to be able to eat three meals, sleep at least five hours a day and pass my exams!


Mohammad SAIF (2014)

I started my career in structural biology two years back during my masters, which made me realize the beauty of crystallography, how complex systems can be studied in their crystal structures by actually viewing them and modifying them for betterment of human life. After graduating from IIT Bombay, I continued my quest in structural biology and joined Bob's lab as an Intern in a structural collaborative project to study methyl transferase enzymes. Under my mentor Dr. Liling and both of my supervisors Dr. Robert Robinson and Dr. Ernesto Guccione, I learned a lot as a budding crystallography student which build up a solid platform for me to further pave my way to develop successful career. Presently I am working on amyloidogenic proteins trying to investigate their role and their method of fibrillation using different structural techniques.

In my free time, I like to travel, running, swimming, listen to calm music and spend my time with my beautiful aquarium.


Mårten LARSSON (2013)

Mårten worked with Bob as a Post Doctoral Fellow from 2006 to 2013.

Currently he is back at Uppsala University, Sweden, where he runs a small mass spectrometry-based proteomics facility, connected to the genomics lab of Leif Andersson. There he tries to perform characterization and functional analyses of proteins derived from molecular genomic studies, with the aim to identify associations between genetic variation and phenotype. His life now revolves around his lovely Orbitrap Fusion. Of course he still stays connected to the BR lab, with different collaboration projects. It also gives him a reason to come back and visit Singapore, Music Man, Circle Star and BR lab. In that order. In his spare time Mårten enjoys all kinds of sports. On TV. In the pub.


Sharon CHEE (2012)

Hi, I am Sharon. I was a research officer working in both Bob’s and Ivana’s groups on a collaboration project to understand the dynamics of gelsolin. I have learnt a lot from Bob and fellow BR lab members and have had lots of fun too! Being in Bob’s lab has sparked my interest in structural biology and I’m currently pursuing that in the p53Lab, working in collaboration with Bob’s group.

In my spare time I enjoy travelling, running, cycling, watching movies, playing pop music on my ukulele and having great company with friends over good food.


Venkatachalam RAJAKANNAN (2010)

Hi I’m Rajakannan, currently an Assistant Professor at the University of Madras and a crystallographer curious on observations. Working 1D [line in the research article] – 2 [to] – 3D [experimental observation], back and forth…
1D-2D-3D ↔ 3D-2D-1D …


Maria Hernandez-Valladares (2009)

Hi there! I worked in Bob's lab from 2005 to 2009. A lot of protein purification and crystallization! AkTA machines, E. coli and the crystallization robot were my best friends in the lab :)
I work now on MS-based phosphoproteomics in Bergen, Norway. Yes life is a bit different here. It rains 320 days a year so the raincoat and trousers are my second skin.
We enjoy the snow and sleep like bears in winter. We hike and try to sleep during the short nights before the sun arises at 3 am in summer! Never tried to sleep without curtains and with sunglasses? This is the place for that!

I wish you a great success in the present projects and in future funding opportunities!

Hugs from Ernesto and I



Qing MA (2009)

Have great interest in dealing with living things, although my university major was pharmaceutical chemistry. Joining Bob’s team gave me the opportunity to pursue to my true interest. Eager in trying to reveal myth of a few calcium activated actin binding proteins made me forget pay and time passed swiftly…although getting precious protein crystals was the most exciting thing - cloning, protein purification, protein characterization and setting up crystals were also great fun. Still remember that I even tried to hold my breath whiling dealing with extremely calcium sensitive apo-gelsolin. Challenging the limits is the fun of science. After that, I worked about 3 years in the field of science education and developed more communication skills.

Now I am a dedicated mum who is trying to understand early childhood education and to catch up with my young daughter’s Japanese learning speed. Looking forward to do something scientific, educational, and maybe multilingual in the future.  


Alvin TUNG (2009)

Joined BR lab back in early 2005 when she was still starting up. Really thankful that Bob accepted me into his lab and I spent the next 4 years learning so much about protein purification and crystallization, mastering the art of actin purification, plus an eye opening trip to the Taiwan Synchrotron. Once again thanks to Bob for being such a nice boss and patient mentor, wishing the lab all the best! Alvin is now with the Singapore Police Force doing investigation work.


Tackey A. Loonchanta (2006)

Hi there, I'm Tackey. I started working with Bob back in year 2003 during my M.Sc. at Uppsala University, Sweden. I had a chance to work at "BR Lab" as a research trainee in 2006, where I was able to quickly get part of my project done and finished my second MSc. from Suranaree University of Technology, Thailand, before Bob sent me on my way to Canada where I graduated with a PhD in Chemistry from The University of British Columbia in 2012.

BR Lab was the fanciest place for Structural Biologist I have ever been in and Bob was my first Protein X-ray Crystallography teacher. My time with Bob, I was working on Gelsolin superfamily proteins along with some of their binding partners for the most part. I always miss my time there.

Settling in Vancouver, Canada, I'm currently starting up my own business while still handling various science projects from time to time.

# LoveScience #LoveBRLab