6AO1

Crystal structure of a beta-lactamase from Burkholderia phymatum

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2017-08-07
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.978560
Spacegroup name	P 1
Unit cell lengths	69.300, 70.800, 82.580
Unit cell angles	90.47, 98.62, 112.46

Refinement procedure

Resolution	35.057 - 1.800
R-factor	0.1641
Rwork	0.164
R-free	0.20060
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5u8o
RMSD bond length	0.006
RMSD bond angle	0.814
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.057	35.057	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.043	0.029	0.353
Rmeas	0.053	0.036	0.441
Total number of observations	375743
Number of reflections	128398	1401	9438
<I/σ(I)>	14.85	31.69	2.72
Completeness [%]	96.8	94	95.7
Redundancy	2.926	2.828	2.539
CC(1/2)	0.998	0.997	0.870

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	18.6 mg/mL BuphA.15997.PS38000 against MCSG screen condition C7 (200 mM calcium chloride, 0.1 M Tris, pH 8.5, 20% PEG4000), cryoprotectant: 15% ethylene glycol, crystal tracking ID 290667h5, unique puck ID cho2-5