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Preparation and initial characterization of crystals of the photoprotein aequorin from Aequorea victoria.
Hannick, L I; Prasher, D C; Schultz, L W; Deschamps, J R; Ward, K B.
Afiliación
  • Hannick LI; Naval Research Laboratory, Washington, D.C. 20375.
Proteins ; 15(1): 103-7, 1993 Jan.
Article en En | MEDLINE | ID: mdl-8451237
Crystals of recombinant aequorin, the photoprotein from the jellyfish Aequorea victoria, have been grown from solutions containing sodium phosphate. The crystals grow as thin plates which diffract to beyond 2.2 A resolution. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 89.1(1), b = 88.4(1), and c = 52.7(1) A. The asymmetric unit contains two molecules. Crystals exposed to calcium ion solutions emit a steady glow and slowly deteriorate, confirming that the crystals consist of a charged, competent photoprotein. This represents the first successful preparation of single crystals of a photoprotein suitable for diffraction analysis.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aequorina / Escifozoos Límite: Animals Idioma: En Revista: Proteins Asunto de la revista: BIOQUIMICA Año: 1993 Tipo del documento: Article Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aequorina / Escifozoos Límite: Animals Idioma: En Revista: Proteins Asunto de la revista: BIOQUIMICA Año: 1993 Tipo del documento: Article Pais de publicación: Estados Unidos