1MBM
NSP4 proteinase from Equine Arteritis Virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 2001-09-20 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 56.612, 60.326, 62.637 |
Unit cell angles | 74.08, 63.30, 66.18 |
Refinement procedure
Resolution | 16.200 * - 2.000 |
R-factor | 0.20726 |
Rwork | 0.204 |
R-free | 0.26100 * |
Structure solution method | MIR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.271 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 16.200 * | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.050 | 0.179 |
Total number of observations | 169296 * | |
Number of reflections | 43171 | 4151 * |
<I/σ(I)> | 22.4 | 6.1 |
Completeness [%] | 95.0 | 91.5 |
Redundancy | 3.9 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | PEG 8000, sodium cirate, ethylene glycol, sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 105K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | PEG2000 MME | 23 (%(w/v)) | |
3 | 1 | reservoir | Tris | 100 (mM) | pH8.5 |
4 | 1 | reservoir | ethylene glycol | 100 (%(w/v)) | |
5 | 1 | reservoir | ammonium acetate | 0.2 (M) |