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.