Crystallization of hemoglobins II and III of the symbiont-harboring clam Lucina pectinata.
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.
Department of Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201, USA.
M A
MA
Doyle
J
J
Vitali
J B
JB
Wittenberg
S N
SN
Vinogradov
D A
DA
Walz
B F
BF
Edwards
P D
PD
Martin