5A0Y
METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER MARBURGENSIS AT 1.1 A RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2014-12-11 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 82.227, 118.300, 122.560 |
| Unit cell angles | 90.00, 91.90, 90.00 |
Refinement procedure
| Resolution | 48.346 - 1.100 |
| R-factor | 0.1117 |
| Rwork | 0.111 |
| R-free | 0.12910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pot |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.649 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.350 | 1.160 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.060 | 0.700 |
| Number of reflections | 937928 | |
| <I/σ(I)> | 10.5 | 1.7 |
| Completeness [%] | 99.3 | 97.8 |
| Redundancy | 3.4 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 27.5% (V/V) PEG 400, 100 MM HEPES PH 7.5, 250 MM MGCL2, AND 200 MM NACL |
