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Biophys J, February 2000, p. 977-981, Vol. 78, No. 2

Low-Resolution Molecular Structures of Isolated Functional Units from Arthropodan and Molluscan Hemocyanin

J. Günter Grossmann,* S. Abid Ali,dagger Dagger Atiya Abbasi,dagger Zafar H. Zaidi,dagger Stanka Stoeva,Dagger Wolfgang Voelter,Dagger and S. Samar Hasnain*

 *CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, England;  dagger HEJ Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan; and  Dagger Physiologisch-Chemisches Institut, Universität Tübingen, 72076 Tübingen, Germany

Synchrotron x-ray scattering measurements were performed on dilute solutions of the purified hemocyanin subunit (Bsin1) from scorpion (Buthus sindicus) and the N-terminal functional unit (Rta) from a marine snail (Rapana thomasiana). The model-independent approach based on spherical harmonics was applied to calculate the molecular envelopes directly from the scattering profiles. Their molecular shapes in solution could be restored at 2-nm resolution. We show that these units represent stable, globular building blocks of the two hemocyanin families and emphasize their conformational differences on a subunit level. Because no crystallographic or electron microscopy data are available for isolated functional units, this study provides for the first time structural information for isolated, monomeric functional subunits from both hemocyanin families. This has been made possible through the use of low protein concentrations (<= 1 mg/ml). The observed structural differences may offer advantages in building very different overall molecular architectures of hemocyanin by the two phyla.

Biophys J, February 2000, p. 977-981, Vol. 78, No. 2
© 2000 by the Biophysical Society   0006-3495/00/02/977/05  $2.00


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