We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6.
- Authors
Morita, Junko; Kato, Kazuki; Mihara, Emiko; Ishitani, Ryuichiro; Takagi, Junichi; Nishimasu, Hiroshi; Aoki, Junken; Nureki, Osamu
- 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%.
- Subjects
GLYCOPROTEINS; CATALYTIC domains; CHOLINE; LYSOPHOSPHATIDYLCHOLINE acyltransferase; CATALYTIC activity; EXPRESSIVE behavior; X-ray crystallography
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 6, p794
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14008929