38MD

Crystal Structure of a Beta-lactamase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-03-02
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	C 1 2 1
Unit cell lengths	150.007, 76.443, 105.058
Unit cell angles	90.00, 108.26, 90.00

Refinement procedure

Resolution	43.270 - 3.000
R-factor	0.2062
Rwork	0.204
R-free	0.24640
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.765
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((2.2_6163: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.880	3.180
High resolution limit [Å]	3.000	3.000
Rmerge	0.152	1.573
Rmeas	0.165	1.696
Rpim	0.063	0.630
Total number of observations	154532
Number of reflections	22812	3671
<I/σ(I)>	8.7
Completeness [%]	99.9	100
Redundancy	6.8	7.2
CC(1/2)	0.997	0.643

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Berkeley B4: 1500 mM Ammonium sulfate, 100 mM Hepes free acid/ Sodium hydroxide pH 7.5 . BuamA.12746.a.B1.PW37793 at 23 mg/mL. plate 13822 E4 drop 1, Puck: OEP_08_10, Cryo: 20% PEG 200 + 80% crystallant