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.
Doyle
M A
MA
Department of Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Vitali
J
J
Wittenberg
J B
JB
Vinogradov
S N
SN
Walz
D A
DA
Edwards
B F
BF
Martin
P D
PD