3I76
The crystal structure of the orthorhombic form of the putative HAD-hydrolase YfnB from Bacillus subtilis bound to magnesium reveals interdomain movement
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-15 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97958 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.685, 67.964, 271.404 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.177 |
Rwork | 0.175 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ed5 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.484 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.097 | 0.397 |
Number of reflections | 51221 | |
<I/σ(I)> | 33.1 | 8.9 |
Completeness [%] | 91.6 | 87.7 |
Redundancy | 6.7 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 294 | 100mM Tris HCl pH 8.5, 30% PEG 4K, 200mM magnesium chloride, vapor diffusion, temperature 294K |