1HCM
Cytochrome cd1 Nitrite Reductase, oxidised from from tetragonal crystals
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 | 2000-10-05 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 128.305, 128.305, 264.825 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.226 * |
Rwork | 0.226 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h9x |
RMSD bond length | 0.012 * |
RMSD bond angle | 1.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.062 | 0.280 |
Number of reflections | 74676 | |
<I/σ(I)> | 17.6 | 3.9 |
Completeness [%] | 98.1 | 91.2 |
Redundancy | 3.1 | 2.8 * |
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 ASCORBATE AND 2.5 UM PMS FROM REDUCTION OF PROTEIN WAS ALSO PRESENT IN CRYSTALLISATION. CRYSTALS WERE GROWN UNDER STRICTLY ANAEROBIC CONDITIONS. THE ENZYME WAS OXIDISED IN THE CRYSTAL BY ALLOWING AIR TO DIFFUSE INTO THE DROP |
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) |