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