2V1L
Structure of the conserved hypothetical protein VC1805 from pathogenicity island VPI-2 of Vibrio cholerae O1 biovar eltor str. N16961 shares structural homology with the human P32 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 78.312, 78.312, 42.288 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.160 - 2.130 |
| R-factor | 0.239 |
| Rwork | 0.235 |
| R-free | 0.31600 |
| Structure solution method | MIRAS |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.386 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SOLVE/RESOLVE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.160 | 2.250 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.060 | 0.380 |
| Number of reflections | 8131 | |
| <I/σ(I)> | 23 | 6.4 |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 8.8 | 9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | pH 7.5 |
