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

Abstract

Further understanding of the structure and function of plasma apolipoproteins requires the determination of their high-resolution structures when complexed with lipids. In these studies, the production of homogeneous, biologically active lipoprotein particles of apolipoprotein E complexed with dipalmitoylphosphatidylcholine and their crystallization and X-ray diffraction are demonstrated. 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 Å resolution.

Authors:
 [1];  [1];  [2];  [1];  [2];  [2]
  1. Gladstone Institutes of Cardiovascular and Neurological Disease, University of California, San Francisco, CA 94158 (United States)
  2. (United States)
Publication Date:
OSTI Identifier:
22356175
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 11; Other Information: PMCID: PMC1978127; PMID: 16511213; PUBLISHER-ID: pu5108; OAI: oai:pubmedcentral.nih.gov:1978127; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BOUND STATE; CRYSTALLIZATION; CRYSTALLOGRAPHY; CRYSTALS; MODULATION; PLASMA; RESOLUTION; X-RAY DIFFRACTION

Citation Formats

Newhouse, Yvonne, Peters-Libeu, Clare, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, Weisgraber, Karl H., E-mail: kweisgraber@gladstone.ucsf.edu, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, and Department of Pathology, University of California, San Francisco, CA 94158. Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105032410.
Newhouse, Yvonne, Peters-Libeu, Clare, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, Weisgraber, Karl H., E-mail: kweisgraber@gladstone.ucsf.edu, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, & Department of Pathology, University of California, San Francisco, CA 94158. Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles. United Kingdom. doi:10.1107/S1744309105032410.
Newhouse, Yvonne, Peters-Libeu, Clare, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, Weisgraber, Karl H., E-mail: kweisgraber@gladstone.ucsf.edu, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, and Department of Pathology, University of California, San Francisco, CA 94158. Tue . "Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles". United Kingdom. doi:10.1107/S1744309105032410.
@article{osti_22356175,
title = {Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles},
author = {Newhouse, Yvonne and Peters-Libeu, Clare and Cardiovascular Research Institute, University of California, San Francisco, CA 94158 and Weisgraber, Karl H., E-mail: kweisgraber@gladstone.ucsf.edu and Cardiovascular Research Institute, University of California, San Francisco, CA 94158 and Department of Pathology, University of California, San Francisco, CA 94158},
abstractNote = {Further understanding of the structure and function of plasma apolipoproteins requires the determination of their high-resolution structures when complexed with lipids. In these studies, the production of homogeneous, biologically active lipoprotein particles of apolipoprotein E complexed with dipalmitoylphosphatidylcholine and their crystallization and X-ray diffraction are demonstrated. 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 Å resolution.},
doi = {10.1107/S1744309105032410},
journal = {Acta Crystallographica. Section F},
number = Pt 11,
volume = 61,
place = {United Kingdom},
year = {Tue Nov 01 00:00:00 EST 2005},
month = {Tue Nov 01 00:00:00 EST 2005}
}