1MRO
METHYL-COENZYME M REDUCTASE
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, Hamburg |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-04 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.720, 116.883, 122.582 |
Unit cell angles | 90.00, 92.02, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.160 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.20700 |
Structure solution method | MIR |
RMSD bond length | 0.013 |
RMSD bond angle | 24.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.3) |
Refinement software | CNS (0.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.230 |
High resolution limit [Å] | 1.160 | 1.160 |
Rmerge | 0.066 | 0.330 |
Number of reflections | 735767 | |
<I/σ(I)> | 18 | 3 |
Completeness [%] | 93.0 | 89 |
Redundancy | 3 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 | 25% PEG 400 0.2 M NACL 20 MG/ML FINAL PROTEIN CONC 0.2 M MGCL 01.M HEPES PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | PEG400 | 25 (%) |