1QLJ
HORSE LIVER ALCOHOL DEHYDROGENASE APO ENZYME DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-04-15 |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.140, 72.920, 180.250 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.226 |
Rwork | 0.226 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hld |
RMSD bond length | 0.010 |
RMSD bond angle | 20.100 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS (0.4) |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.130 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.102 * | 0.221 * |
Total number of observations | 49060 * | |
Number of reflections | 17446 | |
<I/σ(I)> | 5.9 | 3.2 |
Completeness [%] | 94.2 | 87.8 |
Redundancy | 2.8 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 8.4 * | 5 * | PROTEIN WAS CRYSTALLIZED BY THE BATCH DIALYSIS METHOD USING MPD AS THE PRECIPITANT AT PH 7.0, 50 MM AMMONIUM N-[TRIS(HYDROXYMETHYL)METHYL]-2 AMINOETHANESULFONATE, WITH 0.66 MM NADH AND 0.76 MM |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | enzyme | 10 (mg/ml) | |
2 | 1 | 2 | MPD | 4.5 (%) | |
3 | 1 | 2 | tris(hydroxymethyl)aminomethane-HCl | 50 (mM) |