1AMW
ADP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.5 |
| Synchrotron site | SRS |
| Beamline | PX9.5 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-06 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 73.910, 73.910, 111.060 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.850 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.24300 * |
| Structure solution method | ISOMORPHOUS REPLACEMENT |
| Starting model (for MR) | 1ah6 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 25.300 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.000 | 1.890 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.093 * | 0.228 * |
| Number of reflections | 27146 | |
| <I/σ(I)> | 4.6 | 3.2 |
| Completeness [%] | 99.0 | 93.7 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 5 | PROTEIN WAS CRYSTALLIZED UNDER OIL IN TERASAKI PLATES. THE DROPS CONTAINED 27MG/ML PROTEIN, 9.75%(W/V) PEGME 550, 65MM AMMONIUM SULFATE, 32.5MM SODIUM SUCCINATE PH5.0, 5MM ADP AND 5MM MAGNESIUM CHLORIDE., under oil |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 36 (mg/ml) | |
| 2 | 1 | 1 | mPEG550 | 3 (%) | |
| 3 | 1 | 1 | 20 (mM) | ||
| 4 | 1 | 1 | Tris-HCl | 10 (mM) | |
| 5 | 1 | 1 | nucleotide | 5 (mM) | |
| 6 | 1 | 1 | 5 (mM) |
