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Automated Crystal Mounting and Data Collection for Protein Crystallography
- 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.
- Subjects :
- Diffraction
Materials science
Data collection
Data Collection
Drug Storage
Proteins
Nanotechnology
Robotics
Crystallography, X-Ray
Protein Engineering
Synchrotron
Computational science
law.invention
Structural genomics
Crystal
Data acquisition
Structural Biology
law
Drug Design
X-ray crystallography
Crystallization
Protein crystallization
Molecular Biology
Software
Subjects
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