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 |