8HS5
Brucella melitensis 7-alpha-Hydroxysteroid Dehydrogenase mutant: 1-53 truncation-I258M/K262T-NAD+
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-07-12 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9875 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 97.408, 97.408, 92.644 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 24.040 - 2.300 |
| R-factor | 0.1835 |
| Rwork | 0.181 |
| R-free | 0.22740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.952 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.060 | 2.382 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.105 | |
| Rmeas | 0.114 | |
| Number of reflections | 22979 | 22979 |
| <I/σ(I)> | 13.1 | |
| Completeness [%] | 99.7 | |
| Redundancy | 6.1 | |
| CC(1/2) | 0.995 | 0.922 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.1M MIB, 10% PEG3350 |
