1XVS
Crystal structure of apaG Protein from Vibrio cholerae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-08-25 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 0.97940 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.138, 67.998, 64.002 |
| Unit cell angles | 90.00, 131.43, 90.00 |
Refinement procedure
| Resolution | 48.000 - 2.010 |
| R-factor | 0.18426 |
| Rwork | 0.180 |
| R-free | 0.26585 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tza |
| RMSD bond length | 0.038 |
| RMSD bond angle | 2.749 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.100 |
| High resolution limit [Å] | 2.010 | 2.010 |
| Rmerge | 0.112 | 0.267 |
| Number of reflections | 18181 | |
| <I/σ(I)> | 5.6 | |
| Completeness [%] | 94.7 | 77.2 |
| Redundancy | 6.1 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | Bis-Tris, Magnesium, Formate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
