3CAR
REDUCED STRUCTURE OF THE ACIDIC CYTOCHROME C3 FROM DESULFOVIBRIO AFRICANUS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM02 |
Synchrotron site | ESRF |
Beamline | BM02 |
Temperature [K] | 108.2 |
Detector technology | CCD AREA DETECTOR |
Collection date | 1998-01-21 |
Detector | THOMSON/PRINCETON JNSJR |
Spacegroup name | I 2 3 |
Unit cell lengths | 107.657, 107.657, 107.657 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
Rwork | 0.198 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | OXIDISED FORM OF THE SAME PROTEIN |
RMSD bond length | 0.014 |
RMSD bond angle | 0.030 |
Data reduction software | XDS |
Data scaling software | CCP4 |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.000 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.065 * | 0.531 * |
Number of reflections | 17501 | |
<I/σ(I)> | 8.6 | 1.2 |
Completeness [%] | 97.9 | 87.4 |
Redundancy | 32.4 | 13.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.8 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 6-8 (%(w/v)) | |
3 | 1 | reservoir | zinc acetate | 0.05 (M) | |
4 | 1 | reservoir | cacodylate | 0.1 (M) |