1HBM
METHYL-COENZYME M REDUCTASE ENZYME PRODUCT COMPLEX
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-15 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 82.000, 118.300, 122.800 |
Unit cell angles | 90.00, 92.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.800 |
R-factor | 0.164 * |
Rwork | 0.164 |
R-free | 0.19300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mro |
RMSD bond length | 0.014 |
RMSD bond angle | 2.200 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 1.820 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.088 | 0.183 * |
Number of reflections | 198635 | |
<I/σ(I)> | 8.21 | 3.9 |
Completeness [%] | 91.8 | 74.9 |
Redundancy | 4.2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 4 * | 25% PEG 400, 0.2 M NACL, 20 MG/ML FINAL PROTEIN CONC, 0.2 M MGCL, 0.1 M HEPES PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG400 | 20-25 (%) | |
2 | 1 | reservoir | 200 (mM) | ||
3 | 1 | reservoir | 200 (mM) | ||
4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
5 | 1 | reservoir | glycerol | 20 (%(w/w)) | |
6 | 1 | drop | protein | 50 (mg/ml) | |
7 | 1 | drop | Tris-HCl | 10 (mM) |