2VGN
Structure of S. cerevisiae Dom34, a translation termination-like factor involved in RNA quality control pathways and interacting with Hbs1 (SelenoMet-labeled protein)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-03-17 |
Detector | ADSC CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 75.640, 75.640, 324.510 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 13.976 - 2.505 |
R-factor | 0.2097 |
Rwork | 0.210 |
R-free | 0.25060 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.100 |
RMSD bond angle | 1.330 |
Phasing software | SHELXD |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.110 | 0.490 |
Number of reflections | 69296 | |
<I/σ(I)> | 7.3 | 1.75 |
Completeness [%] | 96.4 | 91.1 |
Redundancy | 2.2 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.7 | 7.5% POLYETHYLENE GLYCOL 4000, 50MM NAH2PO4 PH 6.7, 3% XYLITOL |