4WV7
HEAT SHOCK PROTEIN 70 SUBSTRATE BINDING DOMAIN WITH COVALENTLY LINKED NOVOLACTONE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-02-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 67.536, 87.779, 52.453 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 53.530 - 2.420 |
| R-factor | 0.2039 |
| Rwork | 0.200 |
| R-free | 0.27170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yuw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.260 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 87.780 | 2.550 |
| High resolution limit [Å] | 2.420 | 2.420 |
| Rmerge | 0.113 | 0.506 |
| Number of reflections | 12438 | |
| <I/σ(I)> | 12.3 | 3.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.3 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 294 | 10 mg/ml covalently modified protein in 25 mM Tris-HCl, 50 mM NaCl, 1 mM TCEP was mixed 1:1 with reservior solution containing 0.1 M HEPES, pH 7.0, 70% 2-methyl-2,4-pentanediol |
