2WV5
Crystal structure of foot-and-mouth disease virus 3C protease in complex with a decameric peptide corresponding to the VP1-2A cleavage junction with a GLN to Glu substitution at P1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.033, 75.105, 86.303 |
| Unit cell angles | 90.00, 99.26, 90.00 |
Refinement procedure
| Resolution | 56.330 - 2.700 |
| R-factor | 0.236 |
| Rwork | 0.236 |
| R-free | 0.29000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2j92 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.200 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.090 | 0.390 |
| Number of reflections | 16981 | |
| <I/σ(I)> | 8.6 | 3.2 |
| Completeness [%] | 76.1 | 60.8 |
| Redundancy | 2.4 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | SEE PAPER, pH 8 |
