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. 4.4, p. 143

Section 4.4.6. Synchrotron data collection

K. H. Choia*

aDepartment of Biochemistry and Molecular Biology, 6.614C Basic Science, The University of Texas Medical Branch,University Blvd, Galveston, TX 77555–0647, USA
Correspondence e-mail: kychoi@utmb.edu

4.4.6. Synchrotron data collection

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High-brilliance beamlines at modern synchrotrons have significantly reduced the time required for X-ray data collection, and complete data sets can often be collected within minutes. Thus, the time required for crystal mounting and centring is no longer negligible. Automatic crystal mounting and centring allow users to remotely mount crystals for crystal evaluation and data collection without entering the experimental hutch (Manjasetty et al., 2008[link]; Sharff & Jhoti, 2003[link]; Sugahara et al., 2008[link]).

Automated crystal mounting allows the screening of many crystals for diffraction quality and then goes back to the best diffraction-quality crystals for full data collection. The mounting robot picks up frozen crystals in a pin from a Dewar, puts them on a goniometer and retrieves the pin after the diffraction test. The automated crystal-mounting robots have primarily been developed for use at synchrotron sources, although a commercial version of an automatic sample-mounting robot is now available that can be used with a home-source X-ray generator (ACTOR from Rigaku and cryogenic sample changer from Marresearch). Fully automated crystal alignment is not yet available, but semi-automated crystal centring by clicking a mouse to indicate the intended centre of the crystal is used at most beamlines.

References

Manjasetty, B. A., Turnbull, A. P., Panjikar, S., Bussow, K. & Chance, M. R. (2008). Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Proteomics, 8, 612–625.
Sharff, A. & Jhoti, H. (2003). High-throughput crystallography to enhance drug discovery. Curr. Opin. Chem. Biol. 7, 340–345.
Sugahara, M., Asada, Y., Shimizu, K., Yamamoto, H., Lokanath, N. K., Mizutani, H., Bagautdinov, B., Matsuura, Y., Taketa, M., Kageyama, Y., Ono, N., Morikawa, Y., Tanaka, Y., Shimada, H., Nakamoto, T., Yamamoto, M. & Kunishima, N. (2008). High-throughput crystallization-to-structure pipeline at Riken SPring-8 center. J. Struct. Funct. Genomics, 9, 21–28.








































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