8SF3

Crystal Structure of Acetyl-coenzyme A synthetase from Leishmania infantum (AMP, Acetate and CoA bound)

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	2022-03-27
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9795
Spacegroup name	P 21 21 21
Unit cell lengths	59.017, 69.383, 151.619
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.950 - 1.700
R-factor	0.1513
Rwork	0.149
R-free	0.18720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.012
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.21rc1_4924: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	151.620	1.740
High resolution limit [Å]	1.700	1.700
Rmerge	0.128	1.750
Rmeas	0.133	1.817
Rpim	0.037	0.488
Total number of observations	898647	67456
Number of reflections	68961	4971
<I/σ(I)>	12.3	1.8
Completeness [%]	99.5
Redundancy	13	13.6
CC(1/2)	0.998	0.693

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	291	Crystal Screen HT A9: 30% Peg 4K, 0.2M Ammonium Acetate, 0.1M Sodium citrate pH 5.6. LeinA.00629.b.B1.PW39174 at 20 mg/mL. Plate: 13158 well A9 drop 2. Puck: PSL-1408, Cryo: Direct. 2mM AMP and CoA added prior to crystallization. CoA is either disordered or was hydrylozed. Acetate from the crystallization is bound near the AMP.