5VPQ

Crystal structure of 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	2017-03-22
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 2 2 21
Unit cell lengths	94.700, 165.610, 73.920
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.104 - 1.400
R-factor	0.1389
Rwork	0.139
R-free	0.16110
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4c6y
RMSD bond length	0.008
RMSD bond angle	1.070
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]	41.104	41.104	1.440
High resolution limit [Å]	1.400	6.260	1.400
Rmerge	0.045	0.020	0.555
Rmeas	0.049	0.021	0.596
Total number of observations	932366
Number of reflections	114101	1401	8362
<I/σ(I)>	27.32	76.14	3.24
Completeness [%]	100.0	99	100
Redundancy	8.171	7.415	7.581
CC(1/2)	1.000	1.000	0.880

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.2	290	BuphA.00104.a.B1.PS37967 at 22.6mg/ml, mixed 1:1 with Rigaku Reagents MCSG1 A3: 0.2 M NaCl, 0.1M Sodium Phosphate pH 6.2, 10% PEG8000, cryo protected with 25% Ethylene Glycol