1O0Q
Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-04 |
Detector | MARRESEARCH |
Wavelength(s) | 0.98 |
Spacegroup name | H 3 |
Unit cell lengths | 179.900, 179.900, 37.300 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.200 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.23700 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.009 |
RMSD bond angle | 1.560 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.900 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.099 * | 0.241 * |
Total number of observations | 81355 * | |
Number of reflections | 22772 | |
Completeness [%] | 99.7 | 99.9 |
Redundancy | 3.6 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 4 * | Villeret, V., (1997) Protein Sci., 6, 2462. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.0 |
3 | 1 | drop | protein | 15 (mg/ml) |