2NVB
Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-05-14 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.598, 125.008, 167.111 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.600 - 2.800 |
Rwork | 0.217 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ykf |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.085 | 0.430 |
Number of reflections | 40410 | |
<I/σ(I)> | 12 | 2 |
Completeness [%] | 96.5 | 94 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.3 | 298 | 16%(w/v) PEG 4000, 50mM NaCl, 50mM Tris-HCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 8.3 |