Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1

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Title
Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1
Author(s)
S M Bong; S W Yang; J W Choi; Seung Jun Kim; B I Lee
Bibliographic Citation
Acta Crystallographica Section F-Structural Biology, vol. 71, no. 3, pp. 261-265
Publication Year
2015
Abstract
Myotubularin-related protein 1 is a phosphatase that dephosphorylates phospholipids such as phosphatidylinositol 3-phosphate or phosphatidylinositol 3,5-bisphosphate. In this study, human MTMR1 was overexpressed in Escherichia coli, purified and crystallized at 277K using polyethylene glycol 20000 as a precipitant. Diffraction data were collected to 2.0A resolution using synchrotron radiation. The crystals belonged to space group P1, with unit-cell parameters a = 67.219, b = 96.587, c = 97.581A, α = 87.597, β = 86.072, γ = 77.327°. Assuming the presence of four molecules in the asymmetric unit, the calculated Matthews coefficient value was 2.61A3Da-1 and the corresponding solvent content was 52.9%.
Keyword
MTMRmyotubularinphosphatasephosphatidylinositol
ISSN
1744-3091
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S2053230X15000606
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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