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 |
