Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|61|11|981-984
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.61, Iss.11, 2005-11, pp. : 981-984
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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 Å resolution.
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