Crystallization of Hemoglobins II and III of The Symbiont-Harboring Clam Lucina Pectinata

M. A. Doyle, Wayne State University School of Medicine
Jacqueline Vitali, Cleveland State University
J. B. Wittenberg, Albert Einstein College of Medicine
Stanley N. Vinogradov, Wayne State University School of Medicine
D. A. Walz, Wayne State University School of Medicine
B.F. P. Edwards, Wayne State University School of Medicine
Philip D. Martin, Wayne State University

This work was supported in part by NSF grant DCB90-17722 (JBW) and NIH grants GM33192 (BFPE), DK30382 (DAW) and DK38674 (SNV).

Abstract

Diffraction data to 2.7 A resolution were measured on crystals of the homotetramers of components II and III of the cytoplasmic hemoglobin of the symbiont-harboring clam Lucina pectinata. Even though the crystallization conditions are different and the sequence homology of the two hemoglobins is only 63%, the crystals are isomorphous to each other and to the heterotetramer Hb II/III, implying that the residues primarily involved in the intermolecular interactions and responsible for crystal cohesion may be invariant.