1SRV
THERMUS THERMOPHILUS GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 192-336
Summary for 1SRV
Entry DOI | 10.2210/pdb1srv/pdb |
Descriptor | PROTEIN (GROEL (HSP60 CLASS)) (2 entities in total) |
Functional Keywords | chaperone, hsp60, groel, cell division, atp-binding, phosphorylation |
Biological source | Thermus thermophilus |
Total number of polymer chains | 1 |
Total formula weight | 15754.22 |
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 citation | Walsh, 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: 10329779DOI: 10.1107/S0907444999003698 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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