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 |