8SBM
Crystal structure of the wild-type Catalytic ATP-binding domain of Mtb DosS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-12-03 |
| Detector | DECTRIS EIGER2 S 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 54.438, 61.775, 72.234 |
| Unit cell angles | 90.00, 107.54, 90.00 |
Refinement procedure
| Resolution | 34.600 - 1.470 |
| R-factor | 0.155 |
| Rwork | 0.153 |
| R-free | 0.19300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zxo |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.715 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.9) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 34.600 | 34.600 | 1.500 |
| High resolution limit [Å] | 1.470 | 8.050 | 1.470 |
| Rmerge | 0.062 | 0.038 | 0.900 |
| Rmeas | 0.072 | 0.044 | 1.059 |
| Rpim | 0.037 | 0.023 | 0.547 |
| Total number of observations | 143539 | 884 | 6994 |
| Number of reflections | 39045 | 244 | 1934 |
| <I/σ(I)> | 10.8 | 32.3 | 1.1 |
| Completeness [%] | 99.0 | 93.6 | 99.6 |
| Redundancy | 3.7 | 3.6 | 3.6 |
| CC(1/2) | 0.998 | 0.998 | 0.730 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 10 mM ZnCl2, 20% PEG 6000 (w/v), and 100 mM MES (pH 6.0) or 100 mM HEPES (pH 7.2) |
