| Literature DB >> 10329779 |
M A Walsh1, I Dementieva, G Evans, R Sanishvili, A Joachimiak.
Abstract
Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl substituted protein, producing experimental phases to 2.25 A resolution. The data were collected on a mosaic 3 x 3 charge-coupled device using undulator radiation from the Structural Biology Center 19ID beamline at the Argonne National Laboratory's Advanced Photon Source. The phases were independently obtained semiautomatically by two crystallographic program suites, CCP4 and CNS. The quality and speed of this data acquisition exemplify the opportunities at third-generation synchrotron sources for high-throughput protein crystal structure determination.Entities:
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Year: 1999 PMID: 10329779 DOI: 10.1107/s0907444999003698
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449