9EMO

Crystal structure of Histidine acetyltransferase with L-arginine and coenzyme A disulfide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, DESY BEAMLINE P11
Synchrotron site	PETRA III, DESY
Beamline	P11
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-11-15
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	1.033
Spacegroup name	P 63
Unit cell lengths	90.965, 90.965, 99.379
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	45.480 - 1.900
R-factor	0.2233
Rwork	0.223
R-free	0.23850
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.712
Data reduction software	XDS (Jan 31, 2020)
Data scaling software	XDS (Jan 31, 2020)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	78.800	2.020
High resolution limit [Å]	1.900	1.900
Rmeas	0.122	4.060
Number of reflections	72335	11720
<I/σ(I)>	7.51	0.39
Completeness [%]	99.8
Redundancy	5.1
CC(1/2)	0.997	0.178

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	Protein buffer: 10 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, L-Arginine, 0.7 mM Ac-CoA. Well solution: 0.1 M Bis-tris pH 6.8, 20% PEG 3350. Cryo solution: 0.1 M Bis-tris pH 6.8, 20% PEG 3350, 20% Glycerol, 1 mM L-Arginine, 1 mM Ac-CoA