1NPS
CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF PROTEIN S
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 287 |
Detector technology | AREA DETECTOR |
Collection date | 1998-07 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 28.360, 37.940, 37.260 |
Unit cell angles | 90.00, 105.93, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.198 * |
Rwork | 0.200 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 1.800 |
Rmerge | 0.080 |
Number of reflections | 7166 |
Completeness [%] | 99.0 |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 1.4 (mg/ml) | |
2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
3 | 1 | reservoir | PEG10000 | 20 (%(w/v)) |