1AE2
MUTANT L32R 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 | 1995-01 |
| Detector | RIGAKU |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 76.010, 28.030, 42.400 |
| Unit cell angles | 90.00, 103.10, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.223 |
| Rwork | 0.223 |
| R-free | 0.32600 |
| Structure solution method | DIFFERENCE FOURIERS |
| RMSD bond length | 0.019 |
| RMSD bond angle | 27.800 * |
| Data reduction software | R-AXIS (IIC) |
| Data scaling software | R-AXIS (II) |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.200 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.078 | |
| Number of reflections | 5539 | |
| <I/σ(I)> | 9.2 | |
| Completeness [%] | 92.9 | 86.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | PROTEIN WAS CRYSTALLIZED FROM SOLUTIONS CONTAINING 10MG/ML PROTEIN, 4 MM TRIS BUFFER (PH7.5), AND 16% PEG 4000 (W/V), EQUILIBRATED AGAINST 12% PEG4000 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 | PEG4000 | 16 (%(w/v)) | |
| 3 | 1 | drop | Tris-HCl | 4 (mM) | |
| 4 | 1 | reservoir | PEG4000 | 15 (%(w/v)) |






