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Crystallization and preliminary characterization of mitogillin, a ribosomal ribonuclease from Aspergillus restrictus

S E Martinez1, J L Smith

  • 1Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.

Insights

Mitogillin, a fungal ribonuclease, inactivates protein synthesis by cleaving ribosomal RNA. Researchers crystallized mitogillin, enabling X-ray diffraction studies of its structure.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Mitogillin is a ribonuclease produced by Aspergillus restrictus.
  • It targets a conserved sequence in ribosomal RNA, inhibiting protein synthesis.

Purpose of the Study:

  • To crystallize mitogillin for structural analysis.
  • To explore novel crystallization methods using volatile organic solvents.

Main Methods:

  • Mitogillin was crystallized using a two-chamber vapor/liquid diffusion method.
  • Ethanol was employed as the precipitant.
  • X-ray diffraction was used to analyze crystal properties.

Main Results:

  • Mitogillin crystals diffracted X-rays to d-spacings of at least 1.6 A.
  • The crystals belong to the monoclinic space group P2(1).
  • Unit cell parameters were determined: a = 50.4 A, b = 82.4 A, c = 38.2 A, beta = 99.8 degrees.

Conclusions:

  • The crystallization of mitogillin provides a basis for detailed structural studies.
  • The employed crystallization technique demonstrates potential for using volatile organic solvents.
  • Understanding mitogillin's structure can elucidate its mechanism of protein synthesis inhibition.

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