1AM1
ATP 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, 110.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.189 |
Rwork | 0.189 |
Structure solution method | ISOMORPHOUS REPLACEMENT |
Starting model (for MR) | 1ah6 |
RMSD bond length | 0.006 |
RMSD bond angle | 25.700 * |
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 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.116 * | 0.240 * |
Number of reflections | 21414 | |
<I/σ(I)> | 3.3 | 3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 3.5 | 3.5 |
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 ATP 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) |