1QN2
cytochrome cH from Methylobacterium extorquens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF NONIUS |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1997-04-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 33.760, 57.570, 50.950 |
Unit cell angles | 67.81, 89.33, 74.40 |
Refinement procedure
Resolution | 30.000 - 2.010 |
Rwork | 0.161 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2c2c |
RMSD bond length | 0.007 |
RMSD bond angle | 0.018 |
Data reduction software | MOSFLM |
Data scaling software | Agrovata |
Phasing software | CCP4 |
Refinement software | CCP4 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.010 |
Rmerge | 0.061 | 0.134 |
Number of reflections | 16999 | |
<I/σ(I)> | 16.3 | 6.3 |
Completeness [%] | 94.4 | 71.5 |
Redundancy | 2.25 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | HANGING DROP VAPOUR DIFFUSION, 10 MG/ML PROTEIN, 18% PEG 1500, 50 MM TRIS-HCL, PH 7.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG1500 | 18 (%) | |
3 | 1 | reservoir | Tris-HCl | 50 (mM) |