7N7Z

Structure of Acetyl-CoA acetyltransferase from Syntrophomonas wolfei

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-10-15
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 41 21 2
Unit cell lengths	81.070, 81.070, 242.310
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.640 - 2.020
R-factor	0.2369
Rwork	0.233
R-free	0.27420
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4wys
RMSD bond length	0.002
RMSD bond angle	0.480
Data reduction software	XDS (VERSION OCT 15, 2015)
Data scaling software	XSCALE (VERSION OCT 15, 2015)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.640	2.094
High resolution limit [Å]	2.020	2.020
Rmerge	0.104	0.802
Rmeas	0.114	0.893
Rpim	0.046	0.387
Number of reflections	53598	5118
<I/σ(I)>	10.47	1.63
Completeness [%]	99.4	96.93
Redundancy	5.9	5.1
CC(1/2)	0.997	0.511

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	Protein buffer: 20 mM Tris pH 8, 150 mM NaCl, 5 mM B-ME. Crystallization buffer: 0.1 M Sodium formate pH 7.0, 12% PEG 3350. Cryo buffer: 23% PEG 3350, 5% PEG 400.