2XMP
Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP
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 | 80.874, 63.017, 91.107 |
| Unit cell angles | 90.00, 98.84, 90.00 |
Refinement procedure
| Resolution | 29.310 - 2.500 |
| R-factor | 0.209 |
| Rwork | 0.209 |
| R-free | 0.27100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| 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] | 2.590 | 30.000 |
| High resolution limit [Å] | 2.500 | 2.590 |
| Rmerge | 0.090 | 0.290 |
| Number of reflections | 26469 | |
| <I/σ(I)> | 17.6 | 2.85 |
| Completeness [%] | 80.9 | 62.9 |
| Redundancy | 3.9 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 25% PEG3350,0.2M MGCL2,0.1M SODIUM HEPES BUFFER,5MM UDP, pH 8.5 |
