3OSY
Human enterovirus 71 3C protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-05-12 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.288, 75.121, 125.153 |
Unit cell angles | 90.00, 90.11, 90.00 |
Refinement procedure
Resolution | 41.530 - 2.992 |
R-factor | 0.209 |
Rwork | 0.206 |
R-free | 0.25900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vb0 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.066 |
Data reduction software | XDS (PACKAGE) |
Data scaling software | XDS (PACKAGE) |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.000 | 65.000 |
High resolution limit [Å] | 2.990 | 2.990 |
Number of reflections | 19755 | |
Completeness [%] | 93.3 | 79.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.7 | 295 | 200mM Sodium Citrate, 20% PEG3350, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |