7S41

Crystal structure of an N-acetyltransferase from Helicobacter pullorum in the presence of Coenzyme A and dTDP-3-acetamido-3,6-dideoxy-D-glucose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SEALED TUBE
Source details	BRUKER D8 QUEST
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-09-04
Detector	Bruker PHOTON II
Wavelength(s)	1.5418
Spacegroup name	I 2 3
Unit cell lengths	102.965, 102.965, 102.965
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.430 - 1.400
R-factor	0.1638
Rwork	0.163
R-free	0.18260
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7s3u
RMSD bond length	0.010
RMSD bond angle	1.687
Data reduction software	SAINT
Data scaling software	SADABS
Phasing software	REFMAC
Refinement software	REFMAC (5.8.0253)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.500
High resolution limit [Å]	1.400	1.500
Number of reflections	35803	6639
<I/σ(I)>	4.5	4.5
Completeness [%]	100.0	99.9
Redundancy	17.1	11.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	15% PEG-5000, 5 mM dTDP-3-amino-3,6-dideoxy-D-glucose, 5 mM coenzyme A, 100 mM HEPES. Crystals were harvested and soaked in 20% PEG-5000, 200 mM NaCl, 5 mM dTDP-3-amino-3,6-dideoxy-D-glucose, 5 mM acetyl coenzyme A, 100 mM HEPES