1EP5
CRYSTAL STRUCTURE OF THE CONSERVED CORE DOMAIN OF VENEZUALAN EQUINE ENCEPHALITIS CAPSID PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | MACSCIENCE |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-05-24 |
| Detector | MACSCIENCE |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.330, 75.180, 94.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.300 |
| Rwork | 0.228 |
| R-free | 0.26300 |
| RMSD bond length | 1.354 |
| RMSD bond angle | 0.007 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.069 | 0.309 |
| Completeness [%] | 99.0 | 97.9 |
| Redundancy | 13 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.5 | 291 | PEG1000, ammonium sulfate, Bis-Tris, urea, pH 6.5, EVAPORATION, temperature 18K |






