BioMEX is a macromolecular structure solution service currently run out of the Science & Technology Facility Council.
As one of Europe's largest multi-disciplinary research organisations, STFC has access to a network of highly skilled experts who can assist with any stage of the data processing and structure solution service.
Born in Australia, Professor Eleanor Dodson graduated with a degree in mathematics and philosophy from the University of Melbourne. She has played a key role in the development of mathematical and computational techniques to define crystallography.
Eleanor began her career in the 1960s when she was recruited for her mathematical skills to work in the group of the Nobel Prize-winner Dorothy Hodgkin at Oxford, which in 1969 solved the structure of insulin. In 1974, Eleanor along with several others founded a computing cooperative, which in 1979 became CCP4.
Eleanor arrived at York University in 1976 and has been a magnet for other crystallographers who came to work with her at York. It is therefore not surprising that the research group has grown to become the York Structural Biology Laboratory, with around 70 members.
Eleanor has additionally made major contributions to the theory and practice of methods used to determine the atomic structures of macromolecules, such as molecular replacement, phasing and refinement. Her pioneering work to develop analytical tools that allow non-experts to access modern crystallographic techniques led to her election as Fellow of the Royal Society in 2003.
2001 Honorary Degree of Doctor of Science, University of Uppsala
2006 2nd Max Perutz ECA Prize
2010 Honorary Degree of Doctor of Science, University of St Andrews
Using electron-microscopy images as a model for molecular replacement.
E J Dodson, Acta Crystallogr D: Biol Crystallogr, 2001, 57, 1405-1409
Z Dauter, M Dauter and E Dodson E, Acta Crystallogr D: Biol Crystallogr, 2002, 58, 494-506.
Pound-wise but penny-foolish: How well do micromolecules fare in macromolecular refinement?
G J Kleywegt, K Henrick, E J Dodson, D M F van Aalten, Structure, 2003, 11, 1051-1059.
A modified ACORN to solve protein structures at resolutions of 1.7.ANG. or better.
J-X Yao, M M Woolfson, K S Wilson and E J Dodson, Acta Crystallogr D: Biol Crystallogr, 2005, 61, 1465-1475.
Dr. Michail Isupov studied molecular and chemical physics at the Moscow Institute of Physics and Technology. He received his PhD degree in 1994 from the Moscow Institute of Crystallography in the laboratory of Boris Vainstein under the supervision of Emil Harutyunyan and Fred Antson (thesis title ‘Crystallographic Studies of Tryptophanse’).
Michail has additionally spent several months in the York Structural Biology Laboratory working with Guy and Eleanor Dodson and at the EMBL Hamburg outstation working with Keith Wilson and Zbyszek Dauter. Michail’s post-doctoral studies began in 1994 at the University of Exeter, UK working with Jenny Littlechild. He is currently a Senior Research fellow in the Exeter Biosciences department.
Michail has collaborated with Garib Murshudov, Alexei Vagin, Andrey Lebedev and Fred Antson over the years. He is currently working in the field of protein crystallography of macromolecules and is interested in enzymatic catalysis and in methods development for macromolecular structure solution. To date Michail has published over 70 articles in peer-reviewed journals and deposited over 70 structures to the Protein Data Bank. He has expertise in structure solution by MR, MIR, SIRAS and MAD with Se-Met, halogen and intrinsic metal ion scatterers. Michail also has expertise in combining experimental and partial model phases, resolving space group ambiguities and phase improvement by density modification, using NCS features to resolve phase problems.
- Lebedev AA & Isupov MN (2014) Space-group and origin ambiguity in macromolecular structures with pseudo-symmetry and its treatment with the program Zanuda. Acta Crystallogr D70, 2430-2443
- Sayer C, Isupov MN, Westlake A & Littlechild JA (2013) Structural studies of Pseudomonas and Chromobacterium ω-aminotransferases provide insights into their differing substrate specificity. Acta Crystallogr D69, 564-576.
- Lebedev AA, Young P, Isupov MN, Moroz OV, Vagin AA & Murshudov GN (2012) JLigand: a graphical tool for the CCP4 template-restraint library. Acta Crystallogr D68, 431-440.
- Isupov MN & Lebedev AA. (2008) NCS-constrained exhaustive search using oligomeric models. Acta Crystallogr D64, 90-98.
- Vagin AA & Isupov MN (2001) Spherically averaged phased translation function and its applications to search of molecules and fragments in the electron density maps. Acta Crystallogr D57, 1451-1456.
- Winn MD, Isupov MN & Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta crystallogr D57, 122-133.
- Isupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN & Littlechild JA (2000) Crystal structure of dodecameric vanadium dependent bromoperoxidase from the red algae Corallina officinalis. J Mol Biol 299, 1035-1049.
- Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC & Littlechild JA (1999) Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. J Mol Biol 291, 651-660.
- Schroder E, Littlechild JA, Lebedev AA, Errington N, Vagin AA & Isupov MN (2000) Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution. Struct Fold Des 8, 605-615.
- Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G. & Tryggvason K (1999) Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed. Science 284, 1667-1670.
- Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA & Harutyunyan EH (1998) Crystal structure of tryptophanase. J Mol Biol, 276, 603-623.
- Isupov MN, Obmolova G, Butterworth S, Badet-Denisot MA, Badet B, Polikarpov I, Littlechild JA & Teplyakov A (1996) Substrate-binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases - evidence from the 1.8 Å crystal-structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure 4, 801-810.