3LUS
Crystal structure of a putative organic hydroperoxide resistance protein with molecule of captopril bound in one of the active sites from Vibrio cholerae O1 biovar eltor str. N16961
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 | 2009-11-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.203, 76.198, 79.396 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.960 |
| R-factor | 0.17349 |
| Rwork | 0.171 |
| R-free | 0.22697 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3eer |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.758 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.990 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.870 | 0.435 |
| Number of reflections | 17357 | |
| <I/σ(I)> | 30 | 3.5 |
| Completeness [%] | 100.0 | 99.8 |
| Redundancy | 6.8 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 0.1 M sodium Acetate 0.1 M MES 30% Peg 2000MME 30mM captopril 5mM DTT, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
