2WUW
Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile (native data)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX10.1 |
Synchrotron site | SRS |
Beamline | PX10.1 |
Temperature [K] | 287 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.668, 55.314, 75.989 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.720 - 2.230 |
R-factor | 0.18531 |
Rwork | 0.182 |
R-free | 0.24922 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1sca |
RMSD bond length | 0.019 |
RMSD bond angle | 1.856 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.720 | 2.310 |
High resolution limit [Å] | 2.230 | 2.230 |
Rmerge | 0.130 | 0.270 |
Number of reflections | 10557 | |
<I/σ(I)> | 16.6 | 9.2 |
Completeness [%] | 98.2 | 9.2 |
Redundancy | 12.2 | 9.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | SUBTILISIN WAS CRYSTALLIZED BY THE BATCH METHOD FROM BUFFER SOLUTION SATURATED WITH NA2SO4 ABOUT 13% (W/V) AS PRECIPITANT (PETSKO AND TSERNOGLOU 1976). |