5VL0
horse liver alcohol dehydrogenase complexed with NADH and N-benzyformamide
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 | 2006-10-19 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.160, 180.290, 86.920 |
Unit cell angles | 90.00, 106.18, 90.00 |
Refinement procedure
Resolution | 19.950 - 1.200 |
R-factor | 0.1586 |
Rwork | 0.158 |
R-free | 0.19850 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p1r |
RMSD bond length | 0.019 |
RMSD bond angle | 2.061 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.9.9.8L) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.950 | 19.950 | 1.240 |
High resolution limit [Å] | 1.200 | 2.580 | 1.200 |
Rmerge | 0.088 | 0.066 | 0.513 |
Rmeas | 0.094 | 0.070 | 0.576 |
Total number of observations | 2278017 | ||
Number of reflections | 365139 | 23988 | |
<I/σ(I)> | 8.3 | 20.8 | 1.7 |
Completeness [%] | 79.4 | 98.9 | 59.5 |
Redundancy | 6.19 | 8.6 | 4.34 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 7 | 278 | 10 mg/ml enzyme dialyzed against 50 mM ammonium N-[tris(hydroxylmethyl)methyl]2-aminoethane sulfonate (pH 6.7 at 25 deg C) with 1 mM NADH and 10 mM N-benzylformamide as the concentration of 2-methyl-2,4-pentanediol was raised to 25 %. Crystas was mounted on a fiber loop and flash vitrified by plunging it into liquid N2. |