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Updated: Jul 9, 2026
Efficient Mammalian Cell Expression and Single-step Purification of Extracellular Glycoproteins for Crystallization
Published on: December 23, 2015
Expression, purification and crystallization of human 5-lipoxygenase-activating protein with leukotriene-biosynthesis
Shihua Xu1, Brian M McKeever, Douglas Wisniewski
1Department of Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA. shihua_xu@merck.com
Abstract:
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 (P42(1)2) and diffracted to a resolution limit of 4 A.
