1H71
Psychrophilic Protease from Pseudoalteromonas 'TAC II 18'
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 294 |
Detector technology | IMAGE PLATE |
Detector | MAC Science DIP-2030 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.000, 57.550, 161.810 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.100 |
Rwork | 0.164 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kap |
RMSD bond length | 0.017 * |
RMSD bond angle | 3.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.070 | |
Number of reflections | 29234 | |
Completeness [%] | 96.7 | 97.7 |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 4 or 10 * | Villeret, V., (1997) Protein Sci., 6, 2462. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 5-10 (%) | |
2 | 1 | reservoir | 1 (mM) | ||
3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8. |
4 | 1 | drop | protein | 20 (mg/ml) |