International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by E. Arnold, D. M. Himmel and M. G. Rossmann

International Tables for Crystallography (2012). Vol. F, ch. 9.2, p. 231

Section 9.2.1. Introduction

T. Earnesta* and C. Corka

aStructural Proteomics Development Group, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
Correspondence e-mail:  TNEarnest@lbl.gov

9.2.1. Introduction

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The three-dimensional structure of a biological molecule provides fundamental information about how it interacts with other molecules, co-factors and ligands that defines, at a molecular level, how the protein functions in the cellular environment. Protein structure information has also proved to be an invaluable tool in the development of new synthetically derived medicines. The determination of protein structures has significantly accelerated in the past decade, due in large part to advances in protein production (cloning, sequencing, expression and purification), protein crystallography (e.g. cryogenic freezing, intense syn­chrotron X-ray sources, area detectors) and computing. There has been an explosive growth in the use of synchrotron sources for the collection of X-ray diffraction intensities from protein crystals, since synchrotrons can provide bright tunable X-rays which are needed for both high-throughput projects and challenging biomolecular targets such as large complexes and membrane proteins (Wakatsuki & Earnest, 2000[link]).

The convergence of a number of factors in the 1990s and early 2000s motivated the development of robotic crystal mounting – the increase in the number and performance of synchrotron beamlines for biological crystallography, improvements in detector speed, the motorization and computer control of beamlines, advances in computer hardware and software, and an increase in the demand for beam time as structural biologists began to pursue ever more difficult crystallographic projects. Structural genomics efforts and structure-based drug-design programmes benefited significantly, with an increase in the throughput of data collection and analysis for which these systems provided an enabling technology. During the 1990s, the use of cryogenic data collection, instead of mounting in glass capillaries, also allowed synchrotron beamlines to be used more productively, since the bright beams lead very rapidly to the onset of radiation damage unless the crystal is preserved and maintained at low temperatures, typically ∼100–120 K.

References

Wakatsuki, S. & Earnest, T. N. (2000). The impact of synchrotron radiation in protein crystallography. Synchrotron Radiat. News, 13, 4–8.








































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