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 |