2X6Q
Crystal structure of trehalose synthase TreT from P.horikoshi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 297 |
Collection date | 2005-12-01 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 80.788, 63.655, 90.651 |
Unit cell angles | 90.00, 99.41, 90.00 |
Refinement procedure
Resolution | 29.990 - 2.200 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.990 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.080 | 0.340 |
Number of reflections | 41687 | |
<I/σ(I)> | 16.4 | 3.95 |
Completeness [%] | 90.5 | 80.9 |
Redundancy | 3.4 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | PEG 3350 25%, 0.2M MGCL2, 0.1M SODIUM HEPES BUFFER |