4YKQ
Heat Shock Protein 90 Bound to CS301
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-06-13 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97852 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 64.793, 88.934, 99.745 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.190 - 1.910 |
| R-factor | 0.176 |
| Rwork | 0.175 |
| R-free | 0.20090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | In-house APO structure |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.970 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | BUSTER-TNT (BUSTER 2.11.1) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.062 | 0.040 | 0.433 |
| Total number of observations | 119647 | ||
| Number of reflections | 22421 | ||
| <I/σ(I)> | 11.4 | ||
| Completeness [%] | 99.5 | 97.7 | 99.9 |
| Redundancy | 5.3 | 4.9 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 26% Peg 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.0, cryo conditions: 35% Peg 4000, 10% glycerol |
