1. Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1.
- Author
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Bong SM, Yang SW, Choi JW, Kim SJ, and Lee BI
- Subjects
- Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Escherichia coli, Humans, Molecular Sequence Data, Protein Tyrosine Phosphatases, Non-Receptor biosynthesis, Protein Tyrosine Phosphatases, Non-Receptor isolation & purification, Protein Tyrosine Phosphatases, Non-Receptor chemistry
- 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 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 P1, 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%.
- Published
- 2015
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