Literature DB >> 25005088

Crystallization and preliminary X-ray diffraction studies of La1 from Liocheles australasiae.

Saori Kamachi1, Junya Nagao2, Masahiro Miyashita2, Yoshiaki Nakagawa2, Hisashi Miyagawa2, Toshiji Tada1.   

Abstract

A novel scorpion venom peptide, La1 from Liocheles australasiae, with a molecular weight of 7.8 kDa, is presumed to possess a single von Willebrand factor type C (VWC) domain, a common protein module, based on the position of eight Cys residues in its sequence. The biological function of La1 is still unknown. Deciphering its three-dimensional structure will be helpful in understanding its biological function. La1 was crystallized by the sitting-drop vapour-diffusion method using magnesium sulfate as a precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a=63.0, b=30.2, c=32.3 Å, β=108.5°, and diffracted to 1.9 Å resolution. The calculated VM based on one molecule per asymmetric unit was 1.87 Å3 Da(-1). The solvent content was 34.1%.

Entities:  

Keywords:  La1; Liocheles australasiae; venom peptide

Mesh:

Substances:

Year:  2014        PMID: 25005088      PMCID: PMC4089531          DOI: 10.1107/S2053230X14010589

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  14 in total

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8.  Characterization of peptide components in the venom of the scorpion Liocheles australasiae (Hemiscorpiidae).

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