8G41
Horse liver alcohol dehydrogense His-51-Gln form complexed with NADH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU R-AXIS IV |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-05-24 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 44.060, 51.320, 92.750 |
Unit cell angles | 91.90, 103.08, 109.89 |
Refinement procedure
Resolution | 19.910 - 1.500 |
R-factor | 0.15551 |
Rwork | 0.155 |
R-free | 0.17722 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 8g2l |
RMSD bond length | 0.014 |
RMSD bond angle | 1.939 |
Data scaling software | d*TREK (9.9.9.8L) |
Phasing software | REFMAC (5.8.0267) |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.910 | 19.900 | 1.550 |
High resolution limit [Å] | 1.500 | 3.230 | 1.500 |
Rmerge | 0.031 | 0.023 | 0.170 |
Rmeas | 0.036 | 0.026 | 0.199 |
Total number of observations | 45049 | 38068 | |
Number of reflections | 107864 | 11527 | 10037 |
<I/σ(I)> | 25 | 65.6 | 5.7 |
Completeness [%] | 91.2 | ||
Redundancy | 3.84 | 3.87 | 3.75 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 7 | 278 | 10 mg/ml protein in 50 mM ammonium N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfate buffer with 0.25 mM EDTA, 2 mM NAD+ and 0.1 mM 2,2,2-trifluoroetanol, crystals formed at 13 % 2-methyl-2,4-pentanediol, raised to 25% MPD before crystal pliunged into liquid N2. |