3RDW
Putative arsenate reductase from Yersinia pestis
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 | 2011-03-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 132.166, 28.659, 70.118 |
| Unit cell angles | 90.00, 102.87, 90.00 |
Refinement procedure
| Resolution | 33.500 - 2.200 |
| R-factor | 0.2016 |
| Rwork | 0.199 |
| R-free | 0.26260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3f0i |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.710 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 33.400 | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
| Rmerge | 0.117 | 0.060 | 0.625 |
| Number of reflections | 13287 | ||
| <I/σ(I)> | 7.3 | 2 | |
| Completeness [%] | 98.6 | 93.4 | 100 |
| Redundancy | 3.4 | 2.9 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 1.1 M sodium malonate, 0.1 M HEPES buffer, 0.5% Jeffamine ED-2001 Reagent, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
