2CG9
Crystal structure of an Hsp90-Sba1 closed chaperone complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-24 |
| Detector | ADSC CCD |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 126.729, 126.729, 279.777 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 115.470 - 3.100 |
| R-factor | 0.314 |
| Rwork | 0.312 |
| R-free | 0.35300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1HK7 AND 1AMW |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.365 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 3.270 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.190 | 0.460 |
| Number of reflections | 28878 | |
| <I/σ(I)> | 6.7 | 1.3 |
| Completeness [%] | 67.8 | 20.2 |
| Redundancy | 3.3 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | PROTEIN WAS CRYSTALLISED BY THE HANGING DROP METHOD WITH 1:1 DROPS. PROTEIN AT 15MG/ML MIXED WITH 100MM HEPES PH 7.5, 20% PEG4K, 10% ISOPROPANOL, 10% GLYCEROL. |
