1LDE
HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-04 |
Detector | RIGAKU |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.930, 180.200, 86.800 |
Unit cell angles | 90.00, 106.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.205 * |
Rwork | 0.205 |
R-free | 0.25600 |
RMSD bond length | 0.030 |
RMSD bond angle | 0.060 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.035 * | 0.087 * |
Number of reflections | 94632 | |
<I/σ(I)> | 18.8 | 8.8 |
Completeness [%] | 88.8 | 77.2 |
Redundancy | 2.1 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 7 | 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 3-BUTYLTHIOLANE 1-OXIDE. VERY CLOSE TO C-CENTERED ORTHORHOMBIC BUT SCALES VERY BADLY AS C222. SO THE SYMMETRY IS ACTUALLY P21., batch dialysis |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | alcohol dehydrogenase | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfonate | 50 (mM) | |
3 | 1 | reservoir | NADH | 0.66 (mM) | |
4 | 1 | reservoir | N-formylpiperidine | 14 (mM) | |
5 | 1 | reservoir | MPD | 25 (%) |