5V0Z

Crystal structure of Galactoside O-acetyltransferase complex with CoA (P32 space group).

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-07-23
Detector	DECTRIS PILATUS3 X 6M
Wavelength(s)	0.97857
Spacegroup name	P 32
Unit cell lengths	75.434, 75.434, 93.178
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.260
R-factor	0.1375
Rwork	0.136
R-free	0.16420
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5u2k
RMSD bond length	0.014
RMSD bond angle	1.729
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.280
High resolution limit [Å]	1.260	3.420	1.260
Rmerge	0.040	0.034	0.345
Rmeas	0.048	0.040	0.428
Rpim	0.027	0.022	0.250
Number of reflections	159888
<I/σ(I)>	6		2.1
Completeness [%]	99.4	98.8	99.8
Redundancy	2.9	3	2.8
CC(1/2)		0.998	0.925

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289	1uL of 15 mg/ml protein incubated with 5mM CoA were mixed with 1 uL of 25% w/v PEG 3350, 250 mM Sodium/Potassium phosphate, 30% v/v Ethylene glycol and equilibrated against well solution in 15 Well Crystallization Plate (Qiagen).