Open AccessExpression, purification and crystallization of human 5‐lipoxygenase‐activating protein with leukotriene‐biosynthesis inhibitors
Author(s) -
Xu Shihua,
McKeever Brian M.,
Wisniewski Douglas,
Miller Douglas K.,
Spencer Robert H.,
Chu Lin,
Ujjainwalla Feroze,
Yamin TingTing,
Evans Jilly F.,
Becker Joseph W.,
Ferguson Andrew D.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107055571
Subject(s) - arachidonate 5 lipoxygenase , crystallization , chemistry , tetragonal crystal system , recombinant dna , biosynthesis , leukotriene , escherichia coli , lipoxygenase , biochemistry , enzyme , crystallography , biology , crystal structure , organic chemistry , arachidonic acid , gene , asthma , immunology
The nuclear membrane protein 5‐lipoxygenase‐activating protein (FLAP) plays an essential role in leukotriene synthesis. Recombinant full‐length human FLAP with a C‐terminal hexahistidine tag has been expressed and purified from the cytoplasmic membrane of Escherichia coli . Diffraction‐quality crystals of FLAP in complex with leukotriene‐synthesis inhibitor MK‐591 and with an iodinated analogue of MK‐591 have been grown using the sitting‐drop vapor‐diffusion method. The crystals exhibit tetragonal symmetry ( P 42 1 2) and diffracted to a resolution limit of 4 Å.