1SAV
HUMAN ANNEXIN V WITH PROLINE SUBSTITUTION BY THIOPROLINE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 280 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-02 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 |
| Unit cell lengths | 99.600, 99.600, 97.040 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 |
| R-factor | 0.186 |
| Rwork | 0.186 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1avr |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.411 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.550 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.049 | |
| Number of reflections | 12532 | |
| <I/σ(I)> | 9.5 | |
| Completeness [%] | 99.3 | 95.8 |
| Redundancy | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 * | PROTEIN WAS CRYSTALLIZED FROM 2.1 M AMMONIUM SULFATE, 0.1 M TRIS-HCL, PH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9 (mg/ml) | |
| 2 | 1 | drop | Mops | 3 (mM) | |
| 3 | 1 | drop | 20 (mM) | ||
| 4 | 1 | drop | precipitant | 0.0015ml | |
| 5 | 1 | reservoir | ammonium sulfate | 2.1 (M) | |
| 6 | 1 | reservoir | Tris-chloride | 0.1 (M) |
