4H9J
Crystal structure of N-terminal protease (Npro) of classical swine fever virus.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-01 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 60.133, 65.398, 33.315 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.685 - 1.600 |
R-factor | 0.1744 |
Rwork | 0.171 |
R-free | 0.20830 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.123 |
Data reduction software | PROTEUM PLUS (PLUS) |
Data scaling software | PROTEUM PLUS (PLUS) |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.760 | 1.620 |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 18840 | |
<I/σ(I)> | 12.63 | 1.98 |
Completeness [%] | 99.9 | 99.86 |
Redundancy | 34.32 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 290 | 25% PEG3350, 0.2 M (NH4)2SO4 and 0.1 M Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 290K |