5VB0
Crystal structure of fosfomycin resistance protein FosA3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-07-17 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 87.608, 87.608, 357.038 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.753 - 2.689 |
R-factor | 0.2071 |
Rwork | 0.205 |
R-free | 0.24910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5v3d |
RMSD bond length | 0.006 |
RMSD bond angle | 0.973 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.753 | 29.750 | 2.800 |
High resolution limit [Å] | 2.689 | 9.690 | 2.690 |
Rmerge | 0.081 | 0.030 | 0.647 |
Rmeas | 0.085 | 0.032 | 0.683 |
Rpim | 0.028 | 0.011 | 0.218 |
Number of reflections | 39913 | ||
<I/σ(I)> | 20.4 | ||
Completeness [%] | 99.9 | 96.8 | 99.7 |
Redundancy | 9.4 | 7.8 | 9.7 |
CC(1/2) | 0.999 | 0.999 | 0.958 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.95 | 298 | FosA3, protein was concentrated to 9mg/ml and combined with 6mM fosfomycin and 6mM MnCl2. The solution was centrifuged (13500 rpm for 5 minutes) and 250nL of the supernatant was combined with 250nL of mother liquor (7% ethylene glycol, 7% PEG6000, 0.1M HEPES pH 6.95) in sitting drops |