5BRP
Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL15A1 |
Synchrotron site | NSRRC |
Beamline | BL15A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-05-13 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.985 |
Spacegroup name | P 1 |
Unit cell lengths | 60.252, 97.388, 108.539 |
Unit cell angles | 80.30, 88.15, 72.18 |
Refinement procedure
Resolution | 30.000 - 2.050 |
R-factor | 0.1714 |
Rwork | 0.171 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5brq |
RMSD bond length | 0.008 |
RMSD bond angle | 1.091 |
Phasing software | AUTOMAR (1.8.1_1168) |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.050 |
Number of reflections | 141603 |
<I/σ(I)> | 32 |
Completeness [%] | 97.5 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 20% (w/v) PEG 3350, 0.1 M magnesium acetate hexahydrate, 2% Tacsimate (pH 4.0) |