7K3M

Crystal Structure of the Beta Lactamase Class D from Chitinophaga pinensis by Serial Crystallography

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	295
Detector technology	PIXEL
Collection date	2019-11-12
Detector	DECTRIS PILATUS3 X 6M
Wavelength(s)	0.97918
Spacegroup name	P 21 21 21
Unit cell lengths	49.413, 69.347, 70.035
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.280 - 1.800
R-factor	0.1829
Rwork	0.177
R-free	0.22430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	The crystal structure of the same protein in the complex with avibactam which will be deposited
RMSD bond length	0.003
RMSD bond angle	0.580
Data reduction software	DIALS
Data scaling software	PRIME
Phasing software	MOLREP (11.7.02)
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.280	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.670	0.850
Number of reflections	23276	1134
<I/σ(I)>	2.81	0.76
Completeness [%]	100.0	99.8
Redundancy	79.11
CC(1/2)	0.970	0.730

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	295	0.1 M Bis-Tris propane pH 9.0, 8 %(w/v) PEG20000