1H2B
Crystal Structure of the Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Aeropyrum pernix at 1.65A Resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 100.661, 103.186, 67.521 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.620 |
R-factor | 0.16829 |
Rwork | 0.168 |
R-free | 0.20330 * |
Structure solution method | MAD |
Starting model (for MR) | 1hsz |
RMSD bond length | 0.015 * |
RMSD bond angle | 1.746 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.650 |
High resolution limit [Å] | 1.620 | 1.620 |
Rmerge | 0.054 | 0.932 |
Number of reflections | 88078 * | |
<I/σ(I)> | 28.9 | 1.52 |
Completeness [%] | 97.9 | 95.6 |
Redundancy | 11.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.75 | pH 6.75 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PIPES | 100 (mM) | pH6.75 |
2 | 1 | reservoir | PEG600 | 13-16 (%(w/v)) | |
3 | 1 | reservoir | NADH | 0.5 (mM) | |
4 | 1 | drop | protein | 10 (mg/ml) |