title: Crystals of the carboxyl-terminal functional unit from Octopus dofleini hemocyanin.
abstract: The carboxyl-terminal oxygen-binding unit of the polypeptide from Octopus dofleini hemocyanin has been crystallized in a form suitable for three-dimensional X-ray analysis. This proteolytic fragment has a molecular weight of 47 kDa and reversibly binds O2 while exhibiting a slight Bohr effect. Two types of crystals have been grown. Type I crystals, currently under analysis, belong to the orthorhombic space group P2(1)2(1)2(1) and have unit cell dimensions of 92.6 A x 167.4 A x 59.2 A. A composition of two protein molecules per asymmetric unit and 50% solvent content is consistent with a self-rotation function that identifies a non-crystallographic 2-fold axis of symmetry relating these molecules. Diffraction extending beyond 1.9 A Bragg spacings can be detected with synchrotron X-radiation.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
authors.forename: M E
authors.initials: ME
authors.lastname: Cuff
authors.forename: W A
authors.initials: WA
authors.lastname: Hendrickson
authors.forename: J
authors.initials: J
authors.lastname: Lamy
authors.forename: J N
authors.initials: JN
authors.lastname: Lamy
authors.forename: K I
authors.initials: KI
authors.lastname: Miller
authors.forename: K E
authors.initials: KE
authors.lastname: van Holde
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D006433:Hemocyanins; D049831:Octopodiformes; D014961:X-Ray Diffraction
chemical_list: D006433:Hemocyanins