5IHV

Crystal structure of a beta-lactamase 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	2015-11-20
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	49.260, 63.080, 73.850
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.100
R-factor	0.1372
Rwork	0.137
R-free	0.16680
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3w4q
RMSD bond length	0.012
RMSD bond angle	1.285
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (dev_2328)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.130
High resolution limit [Å]	1.100	4.920	1.100
Rmerge	0.049	0.027	0.496
Number of reflections	92835
<I/σ(I)>	18	46.18	2.18
Completeness [%]	98.8	93.5	89.4
Redundancy	5.6
CC(1/2)	0.999

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9.5	290	JCSG+ A7 (267021a7): 100mM CHES pH 9.5, 20% PEG8000, protein conc. 48.83mg/mL; cryo 20% EG; puck uqf3-6