8VWR
Structure of steroid hydratase from Comamonas testosteroni
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-05-09 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.95372 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 95.280, 95.280, 98.590 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.640 - 2.050 |
| R-factor | 0.1984 |
| Rwork | 0.197 |
| R-free | 0.22360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.547 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.19_4092: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.640 | 2.123 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.125 | 3.193 |
| Rmeas | 0.128 | 3.272 |
| Rpim | 0.029 | 0.710 |
| Number of reflections | 32918 | 3235 |
| <I/σ(I)> | 13.81 | 1 |
| Completeness [%] | 100.0 | 99.97 |
| Redundancy | 20 | 21.1 |
| CC(1/2) | 0.999 | 0.492 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277.15 | 1 mcL of reservoir solution (0.1 M sodium cacodylate, 0.2 M calcium acetate hydrate, 40% PEG 300) combined with 1 mcL 30 mM acetyl-CoA and 1 mcL of 20 mg/ml protein |
