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1SRV

THERMUS THERMOPHILUS GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 192-336

Summary for 1SRV
Entry DOI10.2210/pdb1srv/pdb
DescriptorPROTEIN (GROEL (HSP60 CLASS)) (2 entities in total)
Functional Keywordschaperone, hsp60, groel, cell division, atp-binding, phosphorylation
Biological sourceThermus thermophilus
Total number of polymer chains1
Total formula weight15754.22
Authors
Walsh, M.A.,Dementieva, I.,Evans, G.,Sanishvili, R.,Joachimiak, A. (deposition date: 1999-03-02, release date: 1999-03-12, Last modification date: 2023-12-27)
Primary citationWalsh, M.A.,Dementieva, I.,Evans, G.,Sanishvili, R.,Joachimiak, A.
Taking MAD to the extreme: ultrafast protein structure determination.
Acta Crystallogr.,Sect.D, 55:1168-1173, 1999
Cited by
PubMed 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.
PubMed: 10329779
DOI: 10.1107/S0907444999003698
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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