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Science 20 July 2001:
Vol. 293. no. 5529, pp. 519 - 520
DOI: 10.1126/science.293.5529.519
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Tech.Sight

Industrializing Structural Biology

Raymond C. Stevens and Ian A. Wilson

X-ray crystallography is the method of choice for determining molecular structure. The accumulation of molecular structure information has allowed a more complete representation of three-dimensional protein folds, enabling more successful homology modeling of unknown structures. Breakthroughs in genome sequencing projects have underscored the need for concomitant advances in structural biology if we hope to determine the extent of protein folding-space and elucidate how an assembly of proteins constitutes a cellular organism. This essay outlines an industrial approach to high-throughput (HT) determination of molecular structures.

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Structure of a V3-Containing HIV-1 gp120 Core.
C.-c. Huang, M. Tang, M.-Y. Zhang, S. Majeed, E. Montabana, R. L. Stanfield, D. S. Dimitrov, B. Korber, J. Sodroski, I. A. Wilson, et al. (2005)
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High-Throughput Expression of C. elegans Proteins.
C.-H. Luan, S. Qiu, J. B. Finley, M. Carson, R. J. Gray, W. Huang, D. Johnson, J. Tsao, J. Reboul, P. Vaglio, et al. (2004)
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Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.
D. Pantazatos, J. S. Kim, H. E. Klock, R. C. Stevens, I. A. Wilson, S. A. Lesley, and V. L. Woods Jr. (2004)
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Global Efforts in Structural Genomics.
R. C. Stevens, S. Yokoyama, and I. A. Wilson (2001)
Science 294, 89-92
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