1R3D
Crystal structure of protein VC1974 from Vibrio cholerae, Pfam abhydrolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 8-BM |
| Synchrotron site | APS |
| Beamline | 8-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-24 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | .978 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 99.470, 99.470, 53.492 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.18108 |
| Rwork | 0.179 |
| R-free | 0.21554 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.439 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.089 | 0.410 |
| Number of reflections | 21381 | |
| <I/σ(I)> | 18.3 | 6.5 |
| Completeness [%] | 99.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 32% PEG 4000, .1M Tris pH 8.0, 10% Isopropanol, .24M Na Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
