5FBU
Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin-phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-08 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 151.630, 151.630, 191.510 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.633 - 2.850 |
| R-factor | 0.2405 |
| Rwork | 0.238 |
| R-free | 0.29420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5fbt |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.341 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.630 | 2.920 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.078 | 0.736 |
| Number of reflections | 30989 | |
| <I/σ(I)> | 19 | 2.4 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 6.5 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 5 mM rifampin, 5 mM ATP, 35% tacsimate, 10 mM potassium chloride |
