2FXI
Arsenate reductase (ArsC from pI258) C10S/C15A double mutant with sulfate in its active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-03-03 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.591, 33.579, 99.587 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.192 |
| Rwork | 0.189 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ljl |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.310 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.037 | 0.080 |
| Number of reflections | 10780 | |
| <I/σ(I)> | 15.5 | 6.6 |
| Completeness [%] | 97.9 | 83.9 |
| Redundancy | 3.3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 100 mM TRIS ph 8.0, 10 mM DTT, 100 mM KCl, 10 mM K2SO4, 42.5% PEG-4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
