Document Type
Article
Publication Date
9-1-1994
Publication Title
Acta Crystallographica Section D: Biological Crystallography
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.
Repository Citation
Doyle, M. A.; Vitali, Jacqueline; Wittenberg, J. B.; Vinogradov, S. N.; Walz, D. A.; Edwards, B. F.P.; and Martin, P. D., "Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata" (1994). Physics Faculty Publications. 182.
https://engagedscholarship.csuohio.edu/sciphysics_facpub/182
Original Citation
Doyle, M.A., Vitali, J., Wittenberg, J.B., Vinogradov, S.N., Walz, D.A., Edwards, B.F.P. and Martin, P.D. (1994) Crystallization of Hemoglobins II and III of the Symbiont Harboring Clam Lucina Pectinata. Acta Crystallographica D50, 757-759.
DOI
10.1107/S0907444994002556
Version
Publisher's PDF
Publisher's Statement
© 1994 International Union of Crystallography
Volume
D50
Issue
5
Comments
This work was supported in part by NSF grant DCB90-17722 (JBW) and NIH grants GM33192 (BFPE), DK30382 (DAW) and DK38674 (SNV).