5D6O
Orthorhombic Crystal Structure of an acetylester hydrolase from Corynebacterium glutamicum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-26 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.91841 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.141, 89.612, 322.788 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.925 - 1.800 |
R-factor | 0.1754 |
Rwork | 0.175 |
R-free | 0.21030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | trigonal structure of the same protein |
RMSD bond length | 0.003 |
RMSD bond angle | 0.719 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.930 | 1.864 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 120186 | |
<I/σ(I)> | 12.73 | 2.28 |
Completeness [%] | 100.0 | 100 |
Redundancy | 13.1 | 13.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Reservoir: 24 %(w/v) PEG4000, 20 %(v/v) glycerol, 0.16 M magnesium chloride, 80 mM Tris/HCl, pH 8.5. Drop before equilibration: 0.4 mikroliter reservoir solution plut 0.8 mikroliter enzyme solution (protein concentration: 5 mg/ml) |