1FMU
STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-02-06 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 84.606, 84.606, 108.703 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.710 - 2.700 |
| Rwork | 0.208 |
| R-free | 0.27080 * |
| RMSD bond length | 0.015 |
| RMSD bond angle | 27.200 * |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.064 | 0.386 |
| Total number of observations | 78120 * | |
| Number of reflections | 12565 | |
| <I/σ(I)> | 25.7 | |
| Completeness [%] | 97.9 | 96.5 |
| Redundancy | 6.2 | 5.02 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.6 * | 298 | PEG 1500, Ammonium Sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG1500 | 28 (%) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | MES | 0.1 (M) | pH6.0 |
| 4 | 1 | drop | MES | 20 (mM) | pH6.6 |
| 5 | 1 | drop | protein | 5 (mg/ml) |
