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Crystallization and preliminary X‐ray crystallographic analysis of human myotubularin‐related protein 1
Author(s) -
Bong Seoung Min,
Yang Seung Won,
Choi JiWoong,
Kim Seung Jun,
Lee Byung Il
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000606
Subject(s) - polyethylene glycol , crystallization , crystallography , phosphatidylinositol , phosphatase , resolution (logic) , chemistry , x ray crystallography , solvent , molecule , escherichia coli , phosphate , diffraction , materials science , biochemistry , enzyme , phosphorylation , organic chemistry , optics , physics , artificial intelligence , computer science , gene
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 277 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 2.0 Å resolution using synchrotron radiation. The crystals belonged to space group P 1, with unit‐cell parameters a = 67.219, b = 96.587, c = 97.581 Å, 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 2.61 Å 3 Da −1 and the corresponding solvent content was 52.9%.