Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of Enpp6. Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: Morita, Junko; Kato, Kazuki; Mihara, Emiko; Ishitani, Ryuichiro; Takagi, Junichi; Nishimasu, Hiroshi; Aoki, Junken; Nureki, Osamu
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 794
• Page End: 799
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14008929
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>P</italic>1, with unit‐cell parameters <italic>a</italic> = 63.7, <italic>b</italic> = 68.8, <italic>c</italic> = 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%.</p> </abstract>