4DCD
1.6A resolution structure of PolioVirus 3C Protease Containing a covalently bound dipeptidyl inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-10-16 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 56.083, 58.607, 107.991 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.520 - 1.690 |
| R-factor | 0.167 |
| Rwork | 0.166 |
| R-free | 0.18860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l1n |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.308 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHASER (2.3.0) |
| Refinement software | PHENIX (dev_892) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.995 | 1.690 |
| High resolution limit [Å] | 1.690 | 1.600 |
| Number of reflections | 23731 | |
| <I/σ(I)> | 2.3 | |
| Completeness [%] | 99.5 | 99.8 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 30% (w/v) PEG 5000 MME, 100 mM MES, 200 mM ammonium sulfate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
