3BR8
Crystal structure of acylphosphatase from Bacillus subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 26.857, 48.270, 59.567 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.790 - 1.330 |
R-factor | 0.192 |
Rwork | 0.190 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.271 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.300 |
Number of reflections | 66430 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIQUID DIFFUSION | 5.5 | 277 | 50mM phosphate buffer, pH 5.5, LIQUID DIFFUSION, temperature 277K |