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Automated Crystal Mounting and Data Collection for Protein Crystallography

Authors :
Steven W. Muchmore
Vicki L. Nienaber
Jeffrey A. Olson
Sean M. Merrick
Michael Blum
Ronald B. Jones
Peter Magdalinos
Jonathan Greer
Jeff Pan
Source :
Structure. 8:R243-R246
Publication Year :
2000
Publisher :
Elsevier BV, 2000.

Abstract

To increase the efficiency of diffraction data collection for protein crystallographic studies, an automated system designed to store frozen protein crystals, mount them sequentially, align them to the X-ray beam, collect complete data sets, and return the crystals to storage has been developed. Advances in X-ray data collection technology including more brilliant X-ray sources, improved focusing optics, and faster-readout detectors have reduced diffraction data acquisition times from days to hours at a typical protein crystallography laboratory [1, 2]. In addition, the number of high-brilliance synchrotron X-ray beam lines dedicated to macromolecular crystallography has increased significantly, and data collection times at these facilities can be routinely less than an hour per crystal. Because the number of protein crystals that may be collected in a 24 hr period has substantially increased, unattended X-ray data acquisition, including automated crystal mounting and alignment, is a desirable goal for protein crystallography. The ability to complete X-ray data collection more efficiently should impact a number of fields, including the emerging structural genomics field [3], structure-directed drug design, and the newly developed screening by X-ray crystallography [4], as well as small molecule applications.

Details

ISSN :
09692126
Volume :
8
Database :
OpenAIRE
Journal :
Structure
Accession number :
edsair.doi.dedup.....c70afaacd3b53136f1db06a526448ec5
Full Text :
https://doi.org/10.1016/s0969-2126(00)00535-9