5O7N
Beta-lactamase VIM-2 in complex with (2R)-1-(2-Benzyl-3-mercaptopropanoyl)piperidine-2-carboxylic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-09-22 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.989, 79.308, 67.645 |
Unit cell angles | 90.00, 130.45, 90.00 |
Refinement procedure
Resolution | 55.507 - 1.500 |
R-factor | 0.1874 |
Rwork | 0.187 |
R-free | 0.21120 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 0.936 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | AutoSol |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.507 | 1.554 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.076 | 0.541 |
Rpim | 0.047 | 0.338 |
Number of reflections | 128072 | 12879 |
<I/σ(I)> | 10.74 | 2.17 |
Completeness [%] | 99.1 | 99.62 |
Redundancy | 3.6 | 3.6 |
CC(1/2) | 0.998 | 0.763 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 290.15 | The VIM-2 in crystallization buffer (50 mM Tris/HCl pH 7.2, 100 uM ZnCl2 and 150 mM NaCl) was concentrated to 11,4 mg/mL, before 5 % Glycerol was added and the protein was flash frozen in liquid nitrogen. For crystallisation the thrawed protein solutions was mixed with precipitation solution (34% PEG3350, 0,25 M Mg formate, 5 mM BME + 2.5% of a 1M DMSO inhibitor stock in the drop) in differant ratios. As reservoir precipitation solution without inhibitor was used. |