1GU6
Structure of the Periplasmic Cytochrome c Nitrite Reductase from Escherichia coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-02-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 81.472, 90.837, 293.874 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.24300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qdb |
RMSD bond length | 0.020 |
RMSD bond angle | 1.900 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 2.500 | |
Rmerge | 0.089 | 0.244 |
Total number of observations | 1062813 * | |
Number of reflections | 71769 | |
<I/σ(I)> | 5.4 | 2.7 |
Completeness [%] | 93.0 | 94.6 |
Redundancy | 3.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 * | pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | sodium HEPES | 50 (mM) | pH7.0 |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
5 | 1 | reservoir | 2-propanol | 10 (%(v/v)) | |
6 | 1 | reservoir | sodium HEPES | 100 (mM) | pH7.5 |