5OFT
Structural basis for OXA-48 dimerization
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-01-13 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9184 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 120.151, 120.151, 160.107 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.299 - 3.200 |
R-factor | 0.1855 |
Rwork | 0.182 |
R-free | 0.24250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5dtk |
RMSD bond length | 0.006 |
RMSD bond angle | 0.675 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.300 | 3.314 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmeas | 0.185 | |
Number of reflections | 11089 | |
<I/σ(I)> | 8.36 | 2.45 |
Completeness [%] | 93.7 | 96.33 |
Redundancy | 3.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | 14-18% PEG MME 5K and 0.1 M Bis Tris Propane pH 9-9.5. 2 uL hanging drops with a 1:1 ratio between protein and reservoir solution were equilibrated over 1 mL of reservoir solution |