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)) |






