Crystallization and preliminary X-ray crystallographic studies on recombinant human carnitine acetyltransferase.
In this paper, the purification, crystallization and preliminary X-ray crystallographic studies of human carnitine acetyltransferase are reported. Recombinant human carnitine acetyltransferase crystals were grown by the hanging-drop vapor-diffusion method and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 137.65, b = 84.76, c = 57.65 A and one molecule per asymmetric unit. The intensity data were collected from a cryocooled crystal to 1.6 A resolution using a conventional X-ray source.
Lian
Wei
W
Department of Medicinal Chemistry, McKnight Brain Institute and University of Florida, Gainesville 32610, USA.
Govindasamy
Lakshmanan
L
Gu
Yunrong
Y
Kukar
Thomas
T
Agbandje-McKenna
Mavis
M
McKenna
Robert
R
Wu
Donghai
D
D002332:Carnitine O-Acetyltransferase / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D004058:Diffusion; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry*
D011994:Recombinant Proteins; D002332:Carnitine O-Acetyltransferase