6QDL
Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-11-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.124, 114.323, 85.006 |
| Unit cell angles | 90.00, 107.99, 90.00 |
Refinement procedure
| Resolution | 46.704 - 2.929 |
| R-factor | 0.2237 |
| Rwork | 0.221 |
| R-free | 0.26760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4i2z |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.993 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 3.090 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmeas | 0.119 | 0.675 |
| Number of reflections | 20543 | |
| <I/σ(I)> | 8.5 | 1.4 |
| Completeness [%] | 97.0 | 82.3 |
| Redundancy | 3.1 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 292 | 100 mM MES/NaOH pH 6.5 200 mM ammonium acetate 30 % glycerol ethoxylate |
