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

The Results and discussion section reports diffraction data collected to 10–12 Å and maximum resolutions of 10 Å for two crystal forms and 8.5 Å for a third. Those figures support an approximate 10 Å limit for the diffraction data, but the paper does not report a structural model whose resolution was limited to 10 Å. (LLM, conf=0.87)

The Results and discussion report small apoE4–DPPC particles measuring 60 × 80 Å, supporting the particle-size portion of the sentence. The paper does not call them “lipid-poor” or discuss whether their conformation reflects nascent ApoE before further lipidation by ABCA1. (LLM, conf=0.86)

The Results and discussion section reports crystallization and preliminary X-ray diffraction of apoE4–DPPC particles, with two apoE molecules per particle and evidence of twofold symmetry. It does not describe the particles as spheroidal or propose a “horseshoe” conformation; those structural details are not supported by this source. (LLM, conf=0.87)

The Results and discussion section reports two apoE molecules with similar molecular envelopes on the particle surface, which supports part of the proposed arrangement. It does not describe helical domains self-associating or forming a semicircular arc; searches for those terms found no such passage in our copy. No page number is available in the indexed text. (LLM, conf=0.77)

The Results and discussion section reports that dissolved crystals contained intact lipoprotein particles and describes their crystal symmetry, but it does not address whether crystal packing altered the particles’ structure. Searches for crystal packing and structural changes found no passage making that assessment. (LLM, conf=0.72)