2JJC
Hsp90 alpha ATPase domain with bound small molecule fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Collection date | 2004-09-30 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 65.267, 89.019, 99.531 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.160 - 1.950 |
| R-factor | 0.18 |
| Rwork | 0.178 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yer |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.092 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | C-SEARCH |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.000 | 2.010 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.050 | 0.160 |
| Number of reflections | 19531 | |
| <I/σ(I)> | 5.2 | |
| Completeness [%] | 95.0 | 90 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.8 | 0.1M SODIUM CACODYLATE PH 6.8 0.2M MAGNESIUM CHLORIDE 20%(W/V) MPEG 2000 |
