8HS9
Brucella melitensis 7-alpha-Hydroxysteroid Dehydrogenase mutant:I258M/K262T
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) | 0.987 |
| Spacegroup name | P 1 |
| Unit cell lengths | 54.768, 54.813, 76.505 |
| Unit cell angles | 82.94, 70.65, 81.29 |
Refinement procedure
| Resolution | 23.342 - 3.250 |
| R-factor | 0.2429 |
| Rwork | 0.240 |
| R-free | 0.28530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.608 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.342 | 3.370 |
| High resolution limit [Å] | 3.250 | 3.250 |
| Rmerge | 0.182 | 0.462 |
| Rmeas | 0.202 | |
| Number of reflections | 12956 | 12915 |
| <I/σ(I)> | 6.2 | |
| Completeness [%] | 99.9 | |
| Redundancy | 5.4 | |
| CC(1/2) | 0.990 | 0.913 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.2M BIS-TRIS, 15% PEG3350 |
