9EN3

Crystal structure of Histidine acetyltransferase with L-histidine and S-ethyl-coenzyme A

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	2023-06-12
Detector	DECTRIS EIGER2 S 16M
Wavelength(s)	1.033
Spacegroup name	I 2 2 2
Unit cell lengths	49.798, 110.824, 153.819
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.530 - 1.400
R-factor	0.1664
Rwork	0.166
R-free	0.18250
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.080
Data reduction software	XDS (Jan 10, 2022)
Data scaling software	XDS (Jan 10, 2022)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.534	1.480
High resolution limit [Å]	1.400	1.400
Rmeas	0.056	1.410
Number of reflections	160267	25132
<I/σ(I)>	11.4	0.88
Completeness [%]	98.8	95.9
Redundancy	3.8	3.3
CC(1/2)	0.999	0.629

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		281	Protein buffer: 10 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 0.7 mM S-Ethyl-CoA, 0.7 mM L-Histidine. Well solution: 0.1 M HEPES pH 7, 18% PEG 3000. Cryo-solution: 0.1 M Bis-tris pH 6.8, 20% PEG 3000, 25% glycerol, 1 mM S-Ethyl-CoA, 0.7 mM L-Histidine