9EMP

Crystal structure of Histidine acetyltransferase with N-myristoyl histidine and coenzyme A

This is a non-PDB format compatible entry.

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	2020-12-04
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	1.033
Spacegroup name	I 2 2 2
Unit cell lengths	49.929, 111.853, 156.855
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.370 - 1.450
R-factor	0.1885
Rwork	0.188
R-free	0.20940
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.068
Data reduction software	XDS (Jan 31, 2020)
Data scaling software	XDS (Jan 31, 2020)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.19.1_4122)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	91.100	1.540
High resolution limit [Å]	1.450	1.450
Rmeas	0.057	2.670
Number of reflections	75754	11509
<I/σ(I)>	16.41	0.69
Completeness [%]	96.6	91.8
Redundancy	6.7
CC(1/2)	1.000	0.505

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, 1 mM L-Histidine, 0.7 mM Myr-CoA. Well solution: 0.1 M Bis-tris pH 6.8, 22% PEG3350. Cryo solution: 0.1 M Bis-tris pH 6.8, 22% PEG3350, 20% Glycerol