Ma. Doyle et al., CRYSTALLIZATION OF HEMOGLOBIN-II AND HEMOGLOBIN-III OF THE SYMBIONT-HARBORING CLAM LUCINA-PECTINATA, Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 757-759
Diffraction data to 2.7 angstrom resolution were measured on crystals
of the homotetramers of components II and III of the cytoplasmic hemog
lobin 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.