7L52

Crystal Structure of the Metallo Beta Lactamase L1 from Stenotrophomonas maltophilia Determined 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]	297
Detector technology	PIXEL
Collection date	2019-12-10
Detector	DECTRIS PILATUS3 X 6M
Wavelength(s)	0.97918
Spacegroup name	P 64 2 2
Unit cell lengths	105.668, 105.668, 99.332
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.650 - 1.850
R-factor	0.1773
Rwork	0.175
R-free	0.21670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDBID 6UA1
RMSD bond length	0.006
RMSD bond angle	0.761
Data reduction software	DIALS
Data scaling software	cctbx.prime (PRIME)
Phasing software	MOLREP
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.660	1.880
High resolution limit [Å]	1.850	1.850
Number of reflections	28773	1398
<I/σ(I)>	4.08	1.15
Completeness [%]	100.0	100
Redundancy	57.37	29.22
CC(1/2)	0.942	0.818

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	BATCH MODE		289	Batch crystallization done in polypropylene tubes. 200 ul of the L1 (48 mg/ml) in a buffer 0.015 Tris, 0.1 M KCl, 1.5 mM TCEP, 5 mM ZnCl2 pH 7.0 was added to 200 ul of 0.15 M sodium malonate pH 8.0, 20% (w/v) PEG3350.