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Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Sep2014, Vol. 70 Issue 9, p1240-1243, 4p
- Publication Year :
- 2014
-
Abstract
- Myotubularin-related proteins are a large family of phosphatases that have the catalytic activity of dephosphorylating the phospholipid molecules phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. Each of the 14 family members contains a phosphatase catalytic domain, which is inactive in six family members owing to amino-acid changes in a key motif for the activity. All of the members also bear PH-GRAM domains, which have low homologies between them and have roles that are not yet clear. Here, the cloning, expression, purification and crystallization of human myotubularin-related protein 3 encompassing the PH-GRAM and the phosphatase catalytic domain are reported. Preliminary X-ray crystallographic analysis shows that the crystals diffracted to 3.30 Å resolution at a synchrotron X-ray source. The crystals belonged to space group C2, with unit-cell parameters a = 323.3, b = 263.3, c = 149.4 Å, β = 109.7°. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- 9
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 97983145
- Full Text :
- https://doi.org/10.1107/S2053230X14015714