Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Yvonne M NewhouseK H Weisgraber

Abstract

High-resolution structural information is available for several soluble plasma apolipoproteins (apos) in a lipid-free state. However, this information provides limited insight into structure-function relationships, as this class of proteins primarily performs its functions of lipid transport and modulation of lipid metabolism in a lipid-bound state on lipoprotein particles. Here, the possibility of generating homogeneous lipoprotein particles that could be crystallized was explored, opening the possibility of obtaining high-resolution structural information by X-ray crystallography. To test this possibility, apoE4 complexed with the phospholipid dipalmitoylphosphatidylcholine was chosen. Uniform particles containing 50% lipid and 50% apoE4 were obtained and crystallized using the hanging-drop method. Two crystal forms diffract to beyond 8 A resolution.

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Citations

Apr 24, 2013·The Journal of Biological Chemistry·Jobin VarkeyRalf Langen
Oct 4, 2012·Biochimica Et Biophysica Acta·Lei ZhangGang Ren
Jul 6, 2006·Trends in Biochemical Sciences·Danny M HattersKarl H Weisgraber
Feb 20, 2007·Journal of Lipid Research·Clare A Peters-LibeuKarl H Weisgraber
Nov 10, 2005·The Journal of Biological Chemistry·Clare A Peters-LibeuKarl H Weisgraber
Oct 23, 2020·Alzheimer's & Dementia : the Journal of the Alzheimer's Association·Daniel L KoberTom J Brett

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