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Trends and Challenges in Experimental Macromolecular Crystallography

Published online by Cambridge University Press:  17 March 2009

N. E. Chayen
Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, SW7 2BZ, UK
T. J. Boggon
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
A. Cassetta
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
A. Deacon
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
T. Gleichmann
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
J. Habash
Chemistry Department, University of Basle, Switzerland
S. J. Harrop
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
J. R. Helliwell
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
Y. P. Nieh
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
M. R. Peterson
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
J. Raftery
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
E. H. Snell
Chemistry Department, University of Manchester, Manchester, M13 9PL, UK
A. Hädener
Chemistry Department, University of Basle, Switzerland
A. C. Niemann
Chemistry Department, University of Basle, Switzerland
D. P. Siddons
National Synchrotron Light Source, Brookhaven National Laboratory, Upton, USA
V. Stojanoff
National Synchrotron Light Source, Brookhaven National Laboratory, Upton, USA
A. W. Thompson
EMBL, Avenue des Martyrs, Grenoble Cedex, France ESRF, BP220, Grenoble Cedex, France
T. Ursby
ESRF, BP220, Grenoble Cedex, France
M. Wulff
ESRF, BP220, Grenoble Cedex, France


Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 105 proteins that is underway, raises expectations for equivalent three dimensional structural databases.

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Copyright © Cambridge University Press 1996

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