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Quaternary structure of alpha‐crustacyanin from lobster as seen by small‐angle X‐ray scattering
Author(s) -
Dellisanti Cosma D,
Spinelli Silvia,
Cambillau Christian,
Findlay John B.C,
Zagalsky Peter F,
Finet Stéphanie,
Receveur-Bréchot Véronique
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00486-1
Subject(s) - protein quaternary structure , scattering , alpha (finance) , carapace , radius , physics , beta (programming language) , crystallography , small angle scattering , small angle x ray scattering , chemistry , geometry , molecular physics , biology , crustacean , optics , protein subunit , mathematics , biochemistry , zoology , construct validity , statistics , computer security , computer science , gene , programming language , psychometrics
The structure of α‐crustacyanin, the blue carotenoprotein of lobster ( Homarus gammarus ) carapace, has been investigated for the first time using small‐angle X‐ray scattering. In this paper, we have determined the dimensions of this protein composed of eight heterodimeric subunits of β‐crustacyanin. Analysis of the scattering spectra and estimation of the shape of α‐crustacyanin show that the protein fits into a cylinder with an axial length of 238 Å and a radius of 47.5 Å, in which the eight β‐crustacyanin molecules are probably arranged in a helical manner.