2XA9
Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 297 |
Detector technology | CCD |
Collection date | 2005-12-01 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 80.844, 63.139, 91.517 |
Unit cell angles | 90.00, 98.83, 90.00 |
Refinement procedure
Resolution | 29.810 - 2.500 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.600 |
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] | 30.000 | 30.000 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.130 | 0.290 |
Number of reflections | 30955 | |
<I/σ(I)> | 6.1 | 2.2 |
Completeness [%] | 97.2 | 89.1 |
Redundancy | 4.6 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | PEG3350 25%, 0.2M MGCL2, 0.1M SODIUM HEPES BUFFER, 5MM UDPG, pH 8.5 |