5V91
Crystal structure of fosfomycin resistance protein from Klebsiella pneumoniae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-11-21 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 44.875, 67.540, 89.508 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.688 - 1.300 |
R-factor | 0.127 |
Rwork | 0.126 |
R-free | 0.14900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5v3d |
RMSD bond length | 0.007 |
RMSD bond angle | 0.916 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 28.690 |
High resolution limit [Å] | 1.250 |
Rmerge | 0.048 |
Number of reflections | 61827 |
<I/σ(I)> | 19.3 |
Completeness [%] | 81.5 |
Redundancy | 5.7 |
CC(1/2) | 0.999 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | Protein was concentrated to 13mg/ml, and 1ul of protein was combined in hanging drops with 1ul of mother liquor (0.25M MgCl2, 20% PEG3350, 0.1M bis-tris pH 5.5). Resulting crystals were improved by streak seeding |