Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata

M. A. Doyle; Jacqueline Vitali; J. B. Wittenberg; S. N. Vinogradov; D. A. Walz; B. F.P. Edwards; P. D. Martin

doi:10.1107/S0907444994002556

Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata

M. A. Doyle
, Jacqueline Vitali
, J. B. Wittenberg
, S. N. Vinogradov
, D. A. Walz
, B. F.P. Edwards
, P. D. Martin

Wayne State University
Albert Einstein College of Medicine

Research output: Contribution to journal › Article › peer-review

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	https://doi.org/10.1107/S0907444994002556
State	Published - Sep 1 1994

Disciplines

Biochemistry
Biophysics

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Crystallization of Hemoglobins II and III of the Symbiont-HarboriFinal published version, 797 KBLicense: CC BY

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title = "Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata",

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.",

author = "Doyle, \{M. A.\} and Jacqueline Vitali and Wittenberg, \{J. B.\} and Vinogradov, \{S. N.\} and Walz, \{D. A.\} and Edwards, \{B. F.P.\} and Martin, \{P. D.\}",

note = "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.",

year = "1994",

month = sep,

day = "1",

doi = "10.1107/S0907444994002556",

language = "American English",

volume = "D50",

journal = "Acta Crystallographica Section D: Biological Crystallography",

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TY - JOUR

T1 - Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata

AU - Doyle, M. A.

AU - Vitali, Jacqueline

AU - Wittenberg, J. B.

AU - Vinogradov, S. N.

AU - Walz, D. A.

AU - Edwards, B. F.P.

AU - Martin, P. D.

N1 - 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.

PY - 1994/9/1

Y1 - 1994/9/1

N2 - 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.

AB - 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.

UR - https://engagedscholarship.csuohio.edu/sciphysics_facpub/182

U2 - 10.1107/S0907444994002556

DO - 10.1107/S0907444994002556

M3 - Article

VL - D50

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

ER -

Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata

Abstract

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