7AHL
ALPHA-HEMOLYSIN FROM STAPHYLOCOCCUS AUREUS
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-08 |
| Detector | RIGAKU |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 151.920, 136.760, 135.120 |
| Unit cell angles | 90.00, 91.40, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.890 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.25700 |
| Structure solution method | MIR |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.660 |
| Data reduction software | bioteX |
| Data scaling software | bioteX |
| Phasing software | PHASES |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.000 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.080 | 0.083 |
| Total number of observations | 2924665 * | |
| Number of reflections | 206863 | |
| <I/σ(I)> | 8.7 | 3 |
| Completeness [%] | 93.3 | 94.4 |
| Redundancy | 14.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6 | PROTEIN WAS CRYSTALLIZED BY MIXING EQUAL VOLUMES OF A PROTEIN SOLUTION OF 8 MG/ML PROTEIN, 25 MM BETA-OG, 10 MM TRIS AT PH 8.5 AND A PRECIPITANT SOLUTION OF 2.5 M (NH4)2SO4, 0.25% PEG 5K MONOMETHYL ETHER AND 75MM SODIUM CACODYLATE, PH 6.0. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | n-octyl-beta-glucoside | ||
| 2 | 1 | 1 | ammonium sulfate | ||
| 3 | 1 | 1 | mPEG5000 |
