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Trends and Challenges in Experimental Macromolecular Crystallography

Published online by Cambridge University Press:  17 March 2009

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

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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Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 29 , Issue 3 , August 1996 , pp. 227 - 278
Copyright
Copyright © Cambridge University Press 1996

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