2CXV
Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-Derived betaLactone: Selective Crystallization and High-resolution Structure of the His-102 Adduct
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-01-28 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.8857 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.249, 56.022, 80.649 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.350 - 1.400 |
| R-factor | 0.18619 |
| Rwork | 0.166 |
| R-free | 0.18757 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hav |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.986 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.440 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.037 | 0.211 |
| Number of reflections | 39711 | |
| <I/σ(I)> | 13.6 | 5.8 |
| Completeness [%] | 97.7 | 98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 297 | PEG 8000, Tris-HCl, Glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
