Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6

Junko Morita, Kazuki Kato, Emiko Mihara, Ryuichiro Ishitani, Junichi Takagi, Hiroshi Nishimasu, Junken Aoki, Osamu Nureki

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Enpp (ectonucleotide phosphodiesterase/pyrophosphatase) 6 is a membrane-bound glycoprotein that hydrolyzes choline-containing compounds such as lysophosphatidylcholine and glycerophosphorylcholine, and presumably participates in choline metabolism. The catalytic domain of mouse Enpp6 was expressed in HEK293T cells, purified using the TARGET tag/P20.1-Sepharose system and crystallized. An X-ray diffraction data set was collected to 1.8 Å resolution. The crystal belonged to space group P1, with unit-cell parameters a = 63.7, b = 68.8, c = 69.7 Å, α = 60.6, β = 87.0, γ = 68.1°. Assuming the presence of two protein molecules per asymmetric unit, the solvent content was estimated to be 49.5%.

Original languageEnglish
Pages (from-to)794-799
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number6
DOIs
Publication statusPublished - 2014 Jun

Keywords

  • Enpp6
  • N-glycosylation
  • choline

ASJC Scopus subject areas

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

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