3ZZA
Crystal structure of 3C protease of coxsackievirus B3 complexed with alpha, beta-unsaturated ethyl ester inhibitor 84
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 78.380, 63.930, 39.400 |
| Unit cell angles | 90.00, 116.59, 90.00 |
Refinement procedure
| Resolution | 47.230 - 1.800 |
| R-factor | 0.20536 |
| Rwork | 0.203 |
| R-free | 0.25384 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CRYSTAL STRUCTURE OF COXSACKIEVIURS B3 3C PROTEASE |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.906 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.230 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.040 | 0.450 |
| Number of reflections | 15573 | |
| <I/σ(I)> | 14.7 | 3 |
| Completeness [%] | 96.9 | 95.8 |
| Redundancy | 3.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 100 MM TRIS-HCL PH 8.5, 0.2 M MAGNESIUM CHLORIDE, AND 22% PEG 4000; SITTING DROP |
