1H9X
Cytochrome cd1 Nitrite Reductase, reduced form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-06-06 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 127.970, 127.970, 264.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.100 |
R-factor | 0.216 * |
Rwork | 0.216 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aof D1 DOMAIN DIMER |
RMSD bond length | 0.009 * |
RMSD bond angle | 2.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.077 | 0.224 |
Number of reflections | 126324 | |
<I/σ(I)> | 17.6 | 3.9 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | HANGING DROP USING 2.1 M AMMONIUM SULPHATE AND 100 MM CHES PH 7.0 1 MM ASCORMBATE AND 2.5 UM PMS FROM REDUCTION OF PROTEIN WAS ALSO PRESENT IN CRYSTALLISATION. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15-20 (mg/ml) | |
2 | 1 | drop | ascorbate | 2 (mM) | |
3 | 1 | drop | phenazine methosulphate | 0.005 (mM) | |
4 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
5 | 1 | reservoir | CHES | 100 (mM) |