Bergfors, T., Editor. Protein Crystallization: Second Edition. 2009. International
University Line, La Jolla, California, 500 pp.

Bergfors, T., Editor. Protein Crystallization: Techniques, Strategies, and Tips. 1999. International University Line, La Jolla, California, 300 pp.

Journal articles or book chapters
D'Arcy, A., Bergfors, T., Cowan-Jacob, S.W., Marsh, M. Microseed matrix screening for optimization in protein crystallization: what have we learned? Acta Cryst. F70, 1117-1126.

Jansson, A., Bergfors, T., et al., DXR inhibition by potent mono- and disubstituted fosmidomycin analogues. J. Med. Chem. 56, 6190-6199.

Björkelid, C., Bergfors, T., Raichurkar, A.K.V., Mukherjee, K., Malolanarasimhan, K., Bandodkar, B., Jones, T.A. Structural and biochemical characterization of compounds inhibiting Mycobacterium tuberculosis patothenate kinase. J. Biol. Chem. 288, 18260-18270.


Björkelid, C., Bergfors, T., Unge, T., Mowbray, S.L., Jones, T.A. Structural studies on Mycobacterium tuberculosis DXR in complex with the antibiotic FR-900098. Acta Cryst. D68, 134-143.

Fullam, E., Pojer, F., Bergfors, T., Jones, T.A., Cole, S.T. Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme. Open Biology 2, 1-8.

Björkelid, C., Bergfors, T., Henriksson, L.M., Stern, A.L., Unge, T., Mowbray, S.L., Jones, T.A. Structural and functional studies of mycobacterial IspD enzymes. Acta Cryst. D67, 403-414.

Andaloussi, M., Henriksson, L., Wieckowska, A., Lindh, M., Björkelid, C., Larsson, A., Surisetti, S., Iyer, H., Bachally, S., Bergfors, T., Unge, T., Mowbray, S., Larhed, M., Jones, T.A. Karlen, A. Design, synthesis and x-ray crystallographic studies of alpha-aryl substituted fosmidomycin analogues as inhibitors of Mycobacterium tuberculosis 1-deoxy-D-xylulose-5-phosphate reductoisomerase. J. Medicinal Chemistry 54, 4964-4976.

Stojanoff, V., Jakoncic, J., Oren, D.A., Nagarajan, V., Navarro Poulsen, J-C., Adams, Cioaba, M.A., Bergfors, T., Sommer, M.O.A. From screen to structure with a harvestable microfluidic device. Acta Cryst. F67, 971-975.


Bergfors, T. The RAPID crystallization strategy for structure-based inhibitor design. Integrating Crystallography in Drug Discovery. Editor: Sussman, J. Springer Press, 11-19.


Ericsson, D., Kasrayan, A., Johansson, P., Bergfors, T., Sandström, A, Bäckvall, J-E, Mowbray, S. X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation. J. Mol. Biol. 376, 109-119.

Covarrubias, A. S., Högbom, M., Bergfors, T., Carroll, P., Mannerstedt, K., Oscarson, S., Parish, T., Jones, T.A., Mowbray, S. Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis. J. Mol. Biol. 381, 622-633.


Ubhayasekera, W., Tang, C.M., Ho, S., Berglund, G., Bergfors, T., Chye, M-L, and Mowbray, S. Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops. FEBS Letters. 274, 3695-3703.

Bergfors, T. Automated liquid-handling systems for submicroliter crystallization. Protein Crystallization for Structural Genomics. Ed. Chayen, N. International University Line, La Jolla, California.

Bergfors, T. Succeeding with seeding: some practical advice. Evolving Methods for Macromolecular Crystallography. Editors: Read, R. & Sussman, J. Springer Press, 1-10.


Bergfors, T. Crystallization strategy at the Uppsala University RAPID Center. Synchrotron Radiation Science & Technology 13, 5-9.

Bergfors, T. Screening and optimization methods for non-automated crystallization laboratories. Methods Mol. Biol. 363, 131-151.


Covarrubias, A., Larsson, A., Högbom, M., Lindberg, J., Bergfors, T., Björkelid, C., Mowbray, S., Unge, T. and Jones, T.A. Structure and function of carbonic anhydrasses from Mycobacterium tuberculosis. J. Biol. Chem. 280, 18782-18789.

Johansson, P., Unge, T., Cronin, A., Arand, M., Bergfors, T., Jones, T.A. and Mowbray, S. Structure of an atypical epoxide hydrolase from Mycobacterium tuberculosis gives insights into its function. J. Mol. Biol. 351, 1048-1056.

Larsson, A., Bergfors, T., Dultz, E., Irwin, D., Roos, A., Driguez, H, Wilson, D. and
Jones, T.A. Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion. Biochemistry 44, 12915-12922.


Roos, A., Anderson, C.E., Bergfors, T., Jacobsson, M, Karlen, A, Unge, T., Jones, T.A., and Mowbray, S. Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site. J. Mol. Biol. 335, 799-809. 2003

Bergfors, T. Seeds to Crystals. J. Struct. Biol. 142, 66-76.

Johansson, P. Denman, S., Brumer, H., Kallas, Å., Henriksson, H., Bergfors, T., Teeri, T., and Jones, T.A. Crystallization and preliminary X-ray analysis of a xyloglucan endotransglycosylase from Populus tremula x tremuloides. Acta Cryst. D59, 535-537.

Jakobsson, E., Alvite, G., Bergfors, T., Esteves, A., and Kleywegt, G. The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1. BBA-Proteins and Proteonomics 49, 40-50.

Arand, M., Hallberg, B., Zou, J., Bergfors, T., Oesch, F., van der Werf, M., de Bont, J., Jones, T. & Mowbray, S. 1.2 Å structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel mechanism. EMBO J. 22, 2583-2592.

Arand, M., Cronin, A., Oesch, F., Hallberg, M., Zou, JY, Bergfors, T., Mowbray, S., and Jones, T.A. The tell-tale structures of epoxide hydrolases. Drug Metabolism Reviews 35:7 Suppl. 1.


Van Aalten, D.M.F., Milne, K.G., Zou, J.Y., Kleijwegt, G., Bergfors, T., Ferguson, M.A.J., Knudsen, J. and Jones, T.A. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine Acyl-CoA binding protein. J. Mol. Biol. (2001) 309, 181-192.

Zou, J., Hallberg, B.M., Bergfors, T., Oesch, F., Arand, M., Mowbray, S. and Jones, T.A. Structure of Aspergillus niger epoxide hydrolase at 1.8Å resolution: implications for the structure and function of the mammalian microsomal class of epoxide hydrolases. Structure (2000) 8, 111-122.

Hallberg, B.M., Bergfors, T., Backbro, K., Pettersson, G., Henriksson, G., and Divne, C. A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure (2000) 8, 79-88.

Chaudhuri, B.N., Kleywegt, G.J., Broutin-L'Hermite, I., Bergfors, T., Senn, H., Le Motte, P., Partouche, O., and Jones, T.A. Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids. Acta Cryst. (1999) D55, 1850-1857.

Kleywegt, G.J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B., Shudo, K., and Jones, T.A. Crystal structures of cellular retinoid acid binding proteins I and II in complex with all-trans retinoic acid and a synthetic retinoid. Structure (1994) 2:1241-1258.

Bergfors, T., Kleywegt, G.J., and Jones, T.A. Crystallization and X-ray analysis of recombinant bovine cellular retinoic acid binding protein. Acta Cryst. (1994) D50, 370-374.

Uppenberg, J., Patkar, S., Bergfors, T., and Jones, T.A. Crystallization and preliminary studies of lipase B from Candida antarctica . J. Mol. Biol. (1994) 235, 790-792.

Kuehn, M.J., Ogg, D.J., Kihlberg, J., Slonim, L. Flemmer, K., Bergfors, T., and Hultgren, S. Structural basis of pilus subunit recognition by the PapD chaperone. Science (1993) 272, 1234-1241.

Rouvinen, J., Bergfors, T., Teeri, T. and Jones, A. The three dimensional structure of the core protein of cellobiohydrolase II. Science (1990) 249, 380-386.

Jones, T.A., Cowan, S., Newcomer, M. and Bergfors, T. Crystallographic studies on two families of retinoid binding proteins. Frontiers in Drug Research, Alfred Benzon Symposium 28, Munksgaard, Cophenhagen. (1990).

Cowan, S., Bergfors, T., Jones, T.A., Tibbelin, G., Olin, B., Board, P., and Mannervik, B. Crystallization of GST2, a human class alpha glutathione transferase. J. Mol. Biol. (1989) 208, 369-370.

Bergfors, T., Rouvinen, J., Lehtovaara, P., Caldentey, X., Tomme, P., Claeyssens, M., Pettersson, G., Teeri, T., Knowles, J. and Jones, T.A. Crystallization of the core protein of cellobiohydrolase II from Trichoderma reesei. J. Mol. Biol. (1989) 209, 167-169.

Jones, T.A., Bergfors, T., Sedzik, J. and Unge, T. The three dimensional structure of P2 myelin protein. EMBO J. (1988) 7, 1597-1604.

Sedzik, J., Bergfors, T., Jones, T.A. and Weise, M. Bovine P2 myelin basic protein crystallizes in three different forms. J. Neurochem. (1988) 50, 1908-1913.

Bergfors, T., Sedzik, J., Unge, T., Fridborg, K., Weise, M. and Jones, T.A. Crystallization of P2 myelin protein. J. Mol. Biol. (1987) 198, 357-358.

Hultcrantz, R., Ericsson, J. and Hirth, T. Levels of malondialdehyde production in rat liver following loading and unloading with iron. Virchows Arch (Cell Pathol)(1984) 45, 135-146.

Abok, K., Hirth, T., Ericsson, J., and Brunk, U. Effect of iron on the stability of macrophage lysosomes. Virchows Arch (Cell Pathol) (1983) 43, 85-101.

Protein Crystallization Second Edition

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