2VCH
Characterization and engineering of the bifunctional N- and O- glucosyltransferase involved in xenobiotic metabolism in plants
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2006-04-08 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.680, 94.006, 56.992 |
| Unit cell angles | 90.00, 110.24, 90.00 |
Refinement procedure
| Resolution | 53.450 - 1.450 |
| R-factor | 0.179 |
| Rwork | 0.178 |
| R-free | 0.19600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1acv |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.627 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.3.0037) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.450 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.050 | 0.220 |
| Number of reflections | 83274 | |
| <I/σ(I)> | 16.9 | 5.5 |
| Completeness [%] | 99.9 | 99.4 |
| Redundancy | 4.2 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 23 % (W/V) PEG 3350, 0.1 M MMT (MALIC ACID, MES, TRIS BUFFER) PH 8.0 |
