5U2A

Crystal structure of Brucella canis Acyl-CoA Synthetase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2016-05-27
Detector	RAYONIX MX-225
Wavelength(s)	0.979490
Spacegroup name	P 21 21 21
Unit cell lengths	61.600, 92.200, 141.190
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.918 - 2.500
R-factor	0.1926
Rwork	0.191
R-free	0.22830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pg4
RMSD bond length	0.007
RMSD bond angle	0.852
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	PHENIX ((1.11.1_2575: 000))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.560
High resolution limit [Å]	2.500	2.500
Rmerge	0.047	0.512
Number of reflections	28526
<I/σ(I)>	20.27	3.36
Completeness [%]	99.6	99.9
Redundancy	4.8	5
CC(1/2)	0.999	0.944

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	ACETYL COA SYNTHETASE FROM BRUCELLA CANIS ATCC 23365 (BRCAA.00629.A.B1.PW37891) AT 26MG/ML (25 MM TRIS PH 8.0, 200 MM NACL, 1% GLYCEROL, 1 MM TCEP) WAS SET UP IN SPARSE CRYSTALLIZATION TRIALS AT 16C. CRYSTALS WERE PRODUCED BY SITTING DROP VAPOR DIFFUSION WITH AN EQUAL VOLUME OF PROTEIN AND SPARSE SCREEN MORPHEUS CONDITION A9 (0.1M TRIS(BASE), 0.1M BICINE, PH8.5, 0.06M MAGNESIUM CHLORIDE HEXAHYDRATE, 0.06M CALCIUM CHLORIDE DIHYDRATE, 20% PEG500 MME, 10% PEG20,000) AND DIRECTLY CRYO-PROTECTED. CRYSTAL ID 273132A9,RDJ0-10, CLSI-08ID, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K