4L0Q
Crystal structure of S-nitrosoglutathione reductase from Arabidopsis thaliana, C370A/C373A double mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-05-18 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 92.731, 92.731, 173.558 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.650 - 1.950 |
| R-factor | 0.20219 |
| Rwork | 0.200 |
| R-free | 0.25109 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 3uko |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.037 |
| Data reduction software | d*TREK |
| Data scaling software | CrystalClear |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.650 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.091 | 0.440 |
| Number of reflections | 63603 | |
| <I/σ(I)> | 15.6 | 4.4 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 12.1 | 12.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 2.1 M ammonium sulfate, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
