7D5J

CRYSTAL STRUCTURE OF R220A VARIANT PENA BETA-LACTAMASE FROM BURKHOLDERIA MULTIVORANS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE AR-NW12A
Synchrotron site	Photon Factory
Beamline	AR-NW12A
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-12-12
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	1.000
Spacegroup name	C 1 2 1
Unit cell lengths	123.343, 71.158, 84.541
Unit cell angles	90.00, 90.05, 90.00

Refinement procedure

Resolution	42.270 - 1.510
R-factor	0.1747
Rwork	0.174
R-free	0.19280
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3w4q
RMSD bond length	0.005
RMSD bond angle	0.829
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHENIX (1.18.2_3874)
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.270	1.530
High resolution limit [Å]	1.510	1.510
Rmerge	0.056	0.365
Rmeas	0.064	0.427
Rpim	0.056	0.218
Number of reflections	114986	5243
<I/σ(I)>	12.5	2.5
Completeness [%]	99.6	92.5
Redundancy	3.8	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	250microL reservoir (25% polyethylene glycol 8kDa (PEG 8000), 0.1 M MES at pH 6.5)), 4microL hanging drop (7.5 mg/ml protein, 12.5% PEG 8000, 0.05M MES at pH 6.5). Adding Acetone to the drop (final 4%) improved the crystal size and shape.