5NFS
Structure of coxsackievirus B3 3C protease in complex with the alpha-ketoamide (S)-N-benzyl-3-((S)-2-cinnamamido-3-phenylpropanamido)-2-oxo-4-((S)-2-oxopyrrolidin-3-yl)butanamide (cinnamoyl-phenylalanine-GlnLactam-CO-CO-NH-benzyl)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-04-25 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.91841 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.657, 64.354, 39.477 |
| Unit cell angles | 90.00, 115.44, 90.00 |
Refinement procedure
| Resolution | 47.410 - 1.800 |
| R-factor | 0.1817 |
| Rwork | 0.179 |
| R-free | 0.23933 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Ccoxsackievirus B3 3C protease |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.928 |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.410 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.034 | 0.393 |
| Rpim | 0.023 | 0.265 |
| Number of reflections | 16209 | 2332 |
| <I/σ(I)> | 18.9 | |
| Completeness [%] | 99.4 | 99.2 |
| Redundancy | 3.1 | 3 |
| CC(1/2) | 0.999 | 0.887 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M Tris-HCl, 0.2 M MgCl2, pH 8.5, and PEG 3350 varied from 22% to 27% |
