Crystallization and preliminary crystallographic analysis of human LR11 Vps10p domain

Zenzaburo Nakata, Masamichi Nagae, Norihisa Yasui, Hideaki Bujo, Terukazu Nogi, Junichi Takagi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Low-density lipoprotein receptor (LDLR) relative with 11 binding repeats (LR11; also known as sorLA) is genetically associated with late-onset Alzheimers disease and is thought to be involved in neurodegenerative processes. LR11 contains a vacuolar protein-sorting 10 protein (Vps10p) domain. As this domain has been implicated in protein-protein interaction in other receptors, its structure and function are of great biological interest. Human LR11 Vps10p domain was expressed in mammalian cells and the purified protein was crystallized using the hanging-drop vapour-diffusion method. Enzymatic deglycosylation of the sample was critical to obtaining diffraction-quality crystals. Deglycosylated LR11 Vps10p-domain crystals belonged to the hexagonal space group P6122. A diffraction data set was collected to 2.4 Å resolution and a clear molecular-replacement solution was obtained.

Original languageEnglish
Pages (from-to)129-132
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number1
DOIs
Publication statusPublished - Jan 2011
Externally publishedYes

Keywords

  • CHO lec 3.2.8.1 cells
  • LR11
  • Vps10p domain
  • deglycosylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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