4EGK
Human Hsp90-alpha ATPase domain bound to Radicicol
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OTHER |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-20 |
Detector | APEX II CCD |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.440, 43.880, 53.640 |
Unit cell angles | 90.00, 113.81, 90.00 |
Refinement procedure
Resolution | 32.710 - 1.690 |
R-factor | 0.20343 |
Rwork | 0.201 |
R-free | 0.24340 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.019 |
RMSD bond angle | 1.972 |
Data reduction software | PROTEUM2 (suite) |
Data scaling software | PROTEUM2 (suite) |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 32.710 |
High resolution limit [Å] | 1.690 |
Rmerge | 0.037 |
Number of reflections | 25007 |
Redundancy | 3.75 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 273 | 0.2M MgCl2, 0.1M HEPES, 20%w/v PEG2000, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 273K |