2WV9
Crystal Structure of the NS3 protease-helicase from Murray Valley encephalitis virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 293 |
Detector technology | CCD |
Collection date | 2007-05-14 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 41.910, 105.460, 80.068 |
Unit cell angles | 90.00, 97.42, 90.00 |
Refinement procedure
Resolution | 43.940 - 2.750 |
R-factor | 0.268 |
Rwork | 0.267 |
R-free | 0.30000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 2V8O 2ijo |
RMSD bond length | 0.006 |
RMSD bond angle | 0.899 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.937 | 2.820 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.090 | 0.730 |
Number of reflections | 17750 | |
<I/σ(I)> | 19.2 | 3.2 |
Completeness [%] | 99.0 | 98 |
Redundancy | 7.7 | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 100 MM MES PH 6.0, 20% POLYETHYLENE GLYCOL 6000, 200 MM MAGNESIUM CHLORIDE |