5FBT
Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-06-27 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 149.276, 149.276, 193.525 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 24.979 - 2.702 |
R-factor | 0.2252 |
Rwork | 0.223 |
R-free | 0.26030 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.146 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.750 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.063 | 0.708 |
Number of reflections | 35427 | |
<I/σ(I)> | 24.8 | 2.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.6 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | 5 mM rifampin, 0.1 M SPH buffer pH 6, 25% PEG3350 |