Abstract
Diffraction data to 2.7 A resolution were measured on crystals of the homotetramers of components II and III of the cytoplacmic 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.
| Original language | American English |
|---|---|
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | D50 |
| DOIs | |
| State | Published - Sep 1 1994 |
Disciplines
- Biochemistry
- Biophysics