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

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, ?=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%.

SUBMITTER: Kamachi S

PROVIDER: S-EPMC4089531 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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

Kamachi Saori S Nagao Junya J Miyashita Masahiro M Nakagawa Yoshiaki Y Miyagawa Hisashi H Tada Toshiji T

Acta crystallographica. Section F, Structural biology communications 20140618 Pt 7

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 sulfat ...[more]

PMID: 25005088

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