8CON
Crystal structure of alcohol dehydrogenase from Arabidopsis thaliana in complex with NADH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 11.2C |
Synchrotron site | ELETTRA |
Beamline | 11.2C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-09 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.00 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 63.405, 63.405, 182.153 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.020 - 1.700 |
R-factor | 0.187 |
Rwork | 0.186 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 182.150 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.068 | 0.711 |
Rmeas | 0.076 | 0.826 |
Rpim | 0.035 | 0.411 |
Number of reflections | 47829 | 2492 |
<I/σ(I)> | 15.1 | 2.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.5 | 7.3 |
CC(1/2) | 0.999 | 0.827 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.1 M Hepes-NaOH pH 7.0-8.0, 2% v/v PEG 400 and 2.0 M (NH4)2SO4 |