5I0P

Crystal Structure of a Beta-lactamase domain protein from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-12-11
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	45.170, 141.230, 236.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.935 - 2.500
R-factor	0.1686
Rwork	0.166
R-free	0.22850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2zo4
RMSD bond length	0.011
RMSD bond angle	1.211
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MR-Rosetta
Refinement software	PHENIX (dev_2299)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.560
High resolution limit [Å]	2.500	11.180	2.500
Rmerge	0.098	0.041	0.529
Number of reflections	53685
<I/σ(I)>	13.2	28.16	3.01
Completeness [%]	99.9	95.9	100
Redundancy	5.7
CC(1/2)	0.996

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	BuamA.15997.a.B1.PW37786 at 26 mg/ml, protein was mixed 1:1 with Morpheus (a1): 10% (w/v) PEG-20000, 20% (v/v) PEG MME 500, 100 mM MES/imidazole, pH = 6.5, 0.03 M each magnesium chloride, sodium fluoride, sodium bromide, sodium iodide