5Z51
Helicase binding domain of primase from Mycobacterium tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 177 |
| Detector technology | CCD |
| Collection date | 2016-02-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 48.282, 137.559, 36.514 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.492 - 1.583 |
| R-factor | 0.1827 |
| Rwork | 0.181 |
| R-free | 0.20880 |
| Structure solution method | SAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.641 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXCD |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 68.780 | 1.520 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.076 | |
| Rmeas | 0.088 | |
| Rpim | 0.044 | 0.299 |
| Number of reflections | 40035 | |
| <I/σ(I)> | 19.667 | |
| Completeness [%] | 99.6 | 99.8 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.6 | 289 | PEG 3350, magnesium acetate, mops |
