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

Acta Crystallogr F Struct Biol Commun. 2015 Mar;71(Pt 3):261-5. doi: 10.1107/S2053230X15000606. Epub 2015 Feb 19.

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%.

Keywords: MTMR; myotubularin; phosphatase; phosphatidylinositol.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Humans
  • Molecular Sequence Data
  • Protein Tyrosine Phosphatases, Non-Receptor / biosynthesis
  • Protein Tyrosine Phosphatases, Non-Receptor / chemistry*
  • Protein Tyrosine Phosphatases, Non-Receptor / isolation & purification

Substances

  • MTMR1 protein, human
  • Protein Tyrosine Phosphatases, Non-Receptor