6AHI
Crystal structure of O-acetylserine dependent cystathionine beta-synthase from Helicobacter pylori.
Replaces: 5HBGReplaces: 4I1XReplaces: 4R2VExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2011-12-03 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 71.405, 82.719, 96.141 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.120 - 1.900 |
| R-factor | 0.18447 |
| Rwork | 0.183 |
| R-free | 0.20751 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z7w |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.469 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.117 | 0.862 |
| Number of reflections | 45368 | 2244 |
| <I/σ(I)> | 47 | |
| Completeness [%] | 100.0 | |
| Redundancy | 16.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | Peg20K-Peg550MME 15%, 0.09M Amino acids mixture, 0.1M Mes-Imadazole buffer pH 6.5 |
