1P1R
Horse liver alcohol dehydrogenase complexed with NADH and R-N-1-methylhexylformamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-12-09 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.095, 180.340, 87.000 |
| Unit cell angles | 90.00, 106.36, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.570 |
| R-factor | 0.1527 |
| Rwork | 0.152 |
| R-free | 0.20000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hld |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.470 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.27) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.630 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Rmerge | 0.047 | 0.200 * |
| Total number of observations | 636860 * | |
| Number of reflections | 192617 * | |
| <I/σ(I)> | 32.9 | 5.2 |
| Completeness [%] | 94.3 | 79 |
| Redundancy | 3.3 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6.7 * | 4 * | MPD, 50 mM ammonium tris-[(hydroxymethyl)methyl]-2-aminosulfonate buffer, 0.25 mM EDTA, pH 7.0, dialysis, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9.4 (mg/ml) | |
| 2 | 1 | reservoir | ammonium TES | 50 (mM) | pH6.7 |
| 3 | 1 | reservoir | NADH | 1 (mM) | |
| 4 | 1 | reservoir | (R)-N-1-methyl hexyl formamide | 5 (mM) |
