5GTW
The N253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2014-09-21 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 98.383, 134.058, 197.198 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.930 |
| R-factor | 0.18592 |
| Rwork | 0.182 |
| R-free | 0.26676 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4tvu |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.562 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.010 |
| High resolution limit [Å] | 2.910 | 2.910 |
| Rmerge | 0.510 | |
| Number of reflections | 54418 | |
| <I/σ(I)> | 11.8 | 2.1 |
| Completeness [%] | 96.2 | 92.9 |
| Redundancy | 3.6 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 288 | 8% PEG 4000, 0.2M sodium acetate trihydrate, 0.3 M Tris-HCl (pH 7.0) |
