4.0 Article

Expression, purification and preliminary crystallographic analysis of Drosophila melanogaster lysosomal a-mannosidase

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112029375

Keywords

lysosomal a-mannosidases; Drosophila melanogaster; glycosyl hydrolase family 38

Funding

  1. Slovak Research and Development Agency APVV [0117-06]
  2. Ministry of Education of the Slovak Republic
  3. Slovak Academy of Sciences - VEGA [2/0176/11]
  4. Austrian Fonds zur Forderung der wissenschaftlichen Forschung [L314]
  5. Austrian Science Fund (FWF) [L314] Funding Source: Austrian Science Fund (FWF)

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The lysosomal a-mannosidases are class II mannosidases that belong to glycoside hydrolase family 38 and play an important role in the degradation of asparagine-linked carbohydrates of glycoproteins. Based on peptide similarity to human and bovine lysosomal mannosidase (LM), recombinant a-mannosidase from Drosophila melanogaster (dLM408) was cloned and heterologously expressed in Pichia pastoris. The recombinant form of dLM408 designed for structural analysis lacks the transmembrane domain and was crystallized using standard vapour-diffusion and counter-diffusion techniques. The crystals grew as flat plates and as tetragonal bipyramids, respectively. The plate-shaped crystals exhibited the symmetry of space group P212121 and diffracted to a minimum d-spacing of 3.5 angstrom.

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