6NDS

Structure of an HMG-CoA lyase from Acenitobacter baumannii in complex with coenzyme A and 3-methylmalate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-09-02
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.000
Spacegroup name	P 41 21 2
Unit cell lengths	91.460, 91.460, 78.850
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.730 - 1.650
R-factor	0.1541
Rwork	0.153
R-free	0.16770
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	45.730	50.000	1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.057	0.041	0.562
Rmeas	0.061	0.044	0.613
Number of reflections	40790	542	2960
<I/σ(I)>	20.85	42.07	2.91
Completeness [%]	100.0	99.4	99.7
Redundancy	8.605	7.463	6.24
CC(1/2)	0.999	0.998	0.852

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	290	Top96 D11 (298571d11): 2 0.1 M Sodium Acetate: HCl, pH 4.6, 8% (w/v) PEG4000, 4mM NAD (bsi1606), 4mM HMG-CoA (bsi108595); AcbaC.18179.a.B1.PW38191 conc 23.33mg/mL; 20eg; puck/pin ID tud0-16