1E3L
P47H mutant of mouse class II alcohol dehydrogenase complex with NADH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 110 |
Collection date | 1999-01-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.156, 80.639, 102.757 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.500 |
R-factor | 0.1973 |
Rwork | 0.197 |
R-free | 0.25980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cdo |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.9) |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.550 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.068 * | 0.278 * |
Total number of observations | 68302 * | |
Number of reflections | 22033 | |
<I/σ(I)> | 8.2 | 3.1 |
Completeness [%] | 99.0 | 94.7 * |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.3 | pH 8.30 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Bicine | 0.1 (M) | |
2 | 1 | reservoir | NADH | 1 (mM) | |
3 | 1 | reservoir | PEG6000 | 14.0 (%) | |
4 | 1 | drop | protein | 11 (mg/ml) |