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 2.0Å resolution using synchrotron radiation. The crystals belonged to space group P1, with unit-cell parameters a = 67.219, b = 96.587, c = 97.581Å, 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 2.61Å3Da-1 and the corresponding solvent content was 52.9%.
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Bong, S. M., Yang, S. W., Choi, J. W., Kim, S. J., & Lee, B. I. (2015). Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1. Acta Crystallographica Section F: Structural Biology Communications, 71, 261–265. https://doi.org/10.1107/S2053230X15000606
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