1GKH
MUTANT K69H OF GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEIN)
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 285 |
Detector technology | IMAGE PLATE |
Collection date | 1994-01 |
Detector | RIGAKU |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 76.660, 27.750, 41.790 |
Unit cell angles | 90.00, 102.20, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.700 |
R-factor | 0.217 |
Rwork | 0.217 |
R-free | 0.31200 |
Structure solution method | DIFFERENCE FOURIERS |
RMSD bond length | 0.017 |
RMSD bond angle | 27.200 * |
Data reduction software | R-AXIS (IIC) |
Data scaling software | R-AXIS (II) |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.780 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.042 | |
Number of reflections | 7813 | |
<I/σ(I)> | 11 | |
Completeness [%] | 81.4 | 58.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | PROTEIN WAS CRYSTALLIZED FROM SOLUTIONS CONTAINING 10 MG/ML PROTEIN, 4 MM TRIS BUFFER (PH7.5), AND 16% PEG 4000 (W/V), EQUILIBRATED AGAINST 12% PEG 4000 BY VAPOR DIFFUSION AT ROOM TEMPERATURE., vapor diffusion |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 4 (mM) | |
3 | 1 | drop | PEG4000 | 16 (%(w/v)) | |
4 | 1 | reservoir | PEG4000 | 12 (%(w/v)) |