8IYM

Crystal structure of a protein acetyltransferase, HP0935

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	BRUKER AXS MICROSTAR
Temperature [K]	100
Detector technology	CMOS
Collection date	2018-08-18
Detector	BRUKER PHOTON 100
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	117.856, 66.170, 70.904
Unit cell angles	90.00, 91.42, 90.00

Refinement procedure

Resolution	70.880 - 2.000
R-factor	0.2169
Rwork	0.215
R-free	0.24630
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.898
Data reduction software	PROTEUM PLUS
Data scaling software	Aimless (0.7.9)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0405)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	70.880	70.880	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.120	0.058	0.586
Rmeas	0.129	0.062	0.652
Rpim	0.045	0.020	0.283
Total number of observations	273069	4022	14203
Number of reflections	36953	442	2724
<I/σ(I)>	10.4	24.1	2.5
Completeness [%]	99.8	98.8	100
Redundancy	7.4	9.1	5.2
CC(1/2)	0.996	0.997	0.792

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	0.2M potassium thiocyanate, 0.1M Bis-Tris propane pH 6.5, 20% (w/v) polyethylene glycol 3500, 20% (w/v) ethylene glycol (cryo, soaked)