Tables for
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. 233

Section 9.2.3. Conclusion

T. Earnesta* and C. Corka

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

9.2.3. Conclusion

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In summary, the development of automounters over the past decade has been driven by the demands of greater access to synchrotron resources, the need for high-throughput data collection from projects that require numerous structures (e.g. structure-based drug-design and structural genomics programmes) and the demonstrated improvement in data quality for more challenging projects (such as large complexes and membrane proteins) that require the screening of numerous crystals in order to select those with the best diffraction characteristics. A number of different designs have been implemented at synchrotron sources worldwide, to the significant advantage of the structural biology community.

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