2O23
The structure of wild-type human HADH2 (17beta-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-09-01 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 117.037, 117.037, 69.087 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 1.200 |
R-factor | 0.123 |
Rwork | 0.123 |
R-free | 0.15395 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1u7t |
RMSD bond length | 0.012 |
RMSD bond angle | 1.550 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.260 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.092 | |
Number of reflections | 168585 | |
<I/σ(I)> | 8.1 | 1.9 |
Completeness [%] | 99.5 | 99.2 |
Redundancy | 3.6 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 25.5% PEG 3350, 15% glycerol, 0.17 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K |