5MZU
Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-02 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 86.149, 86.149, 716.465 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.400 - 3.800 |
| R-factor | 0.2986 |
| Rwork | 0.298 |
| R-free | 0.31890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.837 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_2645) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.870 |
| High resolution limit [Å] | 3.800 | 10.290 | 3.800 |
| Rmerge | 0.085 | 0.034 | 0.367 |
| Total number of observations | 70085 | ||
| Number of reflections | 16050 | ||
| <I/σ(I)> | 7.4 | ||
| Completeness [%] | 93.5 | 59 | 97.9 |
| Redundancy | 4.4 | 3.2 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 292 | 0.1M Hepes pH 7.0, 10% PEG8000, 12% ethylene glycol |






