5BRQ
Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-11-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.903 |
Spacegroup name | P 1 |
Unit cell lengths | 59.802, 97.584, 108.336 |
Unit cell angles | 98.20, 91.44, 108.15 |
Refinement procedure
Resolution | 24.304 - 2.003 |
R-factor | 0.1817 |
Rwork | 0.181 |
R-free | 0.24530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1uok |
RMSD bond length | 0.008 |
RMSD bond angle | 1.114 |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 149079 |
<I/σ(I)> | 29 |
Completeness [%] | 96.8 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | 20% (w/v) PEG 3350, 0.2 M magnesium acetate hexahydrate, 2% Tacsimate (pH 5.0) |