5WWW
Crystal structure of the KH1 domain of human RNA-binding E3 ubiquitin-protein ligase MEX-3C complex with RNA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-12-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 62 |
| Unit cell lengths | 76.366, 76.366, 36.392 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.183 - 1.798 |
| R-factor | 0.1738 |
| Rwork | 0.172 |
| R-free | 0.20910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dgr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.778 |
| Data reduction software | MOSFLM |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
| Rmerge | 0.159 | 0.121 | 0.705 |
| Rmeas | 0.168 | 0.128 | 0.742 |
| Rpim | 0.053 | 0.042 | 0.229 |
| Total number of observations | 115295 | ||
| Number of reflections | 11406 | ||
| <I/σ(I)> | 3.6 | ||
| Completeness [%] | 99.6 | 99.4 | 98.9 |
| Redundancy | 10.1 | 9.6 | 10.3 |
| CC(1/2) | 0.989 | 0.865 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 5% v/v Tacsimate pH 7.0, 0.1M HEPES pH 7.0, 10% w/v polyethylene glycol monomethyl ether 2000 |
