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Hissa, DC; Bezerra, GA; Obrist, B; Birner-Grünberger, R; Melo, VM; Gruber, K.
Crystallization and preliminary X-ray diffraction of the surfactant protein Lv-ranaspumin from the frog Leptodactylus vastus.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012; 68(Pt 3):321-323 Doi: 10.1107/S1744309112002679 [OPEN ACCESS]
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Co-Autor*innen der Med Uni Graz
Birner-Grünberger Ruth
Obrist Britta
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Abstract:
Lv-ranaspumin is a natural surfactant protein with a molecular mass of 23.5 kDa which was isolated from the foam nest of the frog Leptodactylus vastus. Only a partial amino-acid sequence is available for this protein and it shows it to be distinct from any protein sequence reported to date. The protein was purified from the natural source by ion-exchange and size-exclusion chromatography and was crystallized by sitting-drop vapour diffusion using the PEG/Ion screen at 293 K. A complete data set was collected to 3.5 Å resolution. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 51.96, b = 89.99, c = 106.00 Å. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be 54%. © 2012 International Union of Crystallography
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Anura -
Crystallization -
Crystallography, X-Ray -
Membrane Proteins - chemistry

Find related publications in this database (Keywords)
Leptodactylus vastus
Lv-ranaspumin
surfactant proteins
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