1OA1
REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-15 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.053, 67.464, 134.955 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.500 - 1.550 |
R-factor | 0.132 |
Rwork | 0.131 |
R-free | 0.15300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB FROM ANAEROBILLY AS-ISOLATED HCP PROTEIN 1.35A (D.ARAGAO PRIVATE COMMUNICATION) |
RMSD bond length | 0.011 * |
RMSD bond angle | 1.292 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.500 | 1.590 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.071 | 0.254 |
Total number of observations | 262651 * | |
Number of reflections | 81856 | |
<I/σ(I)> | 13.2 | 3.6 |
Completeness [%] | 95.7 | 93.5 |
Redundancy | 3.2 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 | 277 | 25 PEG 4000 0.1M MES PH 6.5, TEMPERATURE 277 KELVIN |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 25 (%) | |
2 | 1 | reservoir | MES | 0.1 (M) | pH6.5 |
3 | 1 | drop | protein | 25 (mg/ml) | |
4 | 1 | drop | Tris-HCl | 20 (mM) | pH7.6 |
5 | 1 | drop | 0.05 (M) |