3O0H
Crystal structure of glutathione reductase from Bartonella henselae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-13 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.470, 64.650, 90.190 |
| Unit cell angles | 90.00, 107.24, 90.00 |
Refinement procedure
| Resolution | 43.760 - 1.900 |
| R-factor | 0.167 |
| Rwork | 0.164 |
| R-free | 0.20900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2tpr modified with CCP4 program CHAINSAW |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.514 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.049 | 0.278 |
| Number of reflections | 72215 | |
| <I/σ(I)> | 16.03 | 2.7 |
| Completeness [%] | 98.3 | 92.4 |
| Redundancy | 3 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 290 | JCSG+ SCREEN #H8: 200MM NACL, 100MM BISTRIS PH 5.5, 25% PEG 3350; BAHEA.00239.A AT 29.3MG/ML, PH N/A, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |
