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Automation of X-ray crystallography

Abstract

Structure-based biological discovery is entering a new era with the development of industrialized macromolecular structure determination pipelines. Intense, highly focused X-rays from integrated synchrotron radiation beam lines combined with significant advances in protein expression, purification, and micro-crystallization automation allow for the full streamlining of the traditionally tedious and time consuming process of determining the three dimensional structures of macromolecules.

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Figure 1: On the left is the 96-sample cassette, which holds and retains flash-cooled crystals at liquid nitrogen temperatures.
Figure 2: 'Hutch' window of BLU-ICE showing the intuitive interface that allows the experimenter to interact with the synchrotron beam line instrumentation.
Figure 3: Autocentering of protein crystals at the Advanced Light Source.

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Acknowledgements

We appreciate the use of material presented at the SSRL workshop on automation development for synchrotron beam lines held May 11-12, 2000, and information from the 8th International Conference on the Crystallization of Biological Macromolecules (ICCBM8) held in Sandestin, Florida; May 14-19, 2000. In particular, we appreciate the material from S. Muchmore and B.C Wang that was presented in this review. We are grateful to M. Scott for careful reading and helpful discussions of this review. The SSRL and ALS structural biology programs are supported by NIH (NCRR, NIGMS) and the DOE (BES, BER).

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Correspondence to Raymond C. Stevens.

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Abola, E., Kuhn, P., Earnest, T. et al. Automation of X-ray crystallography. Nat Struct Mol Biol 7 (Suppl 11), 973–977 (2000). https://doi.org/10.1038/80754

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