Literature DB >> 3681992

Crystals of Lumbricus erythrocruorin.

W E Royer1, W A Hendrickson, W E Love.   

Abstract

Lumbricus terrestris erythrocruorin, a 3.9 X 10(6) Mr respiratory protein, has been crystallized in four different forms. Despite the high molecular symmetry apparent from images in electron micrographs, only one crystal form expresses any molecular symmetry as crystallographic symmetry. The lattice parameters provide upper limits on the molecular dimensions of 267 A X 308 A X 172 A (1 A = 0.1 nm), which agree well with dimensions obtained from electron micrographs of negatively stained molecules. We have collected diffraction data to 5.5 A from type III crystals and have begun a structural analysis.

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Year:  1987        PMID: 3681992     DOI: 10.1016/0022-2836(87)90618-8

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  3 in total

1.  Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids.

Authors:  W E Royer; K Strand; M van Heel; W A Hendrickson
Journal:  Proc Natl Acad Sci U S A       Date:  2000-06-20       Impact factor: 11.205

2.  Carbohydrate gluing, an architectural mechanism in the supramolecular structure of an annelid giant hemoglobin.

Authors:  S Ebina; K Matsubara; K Nagayama; M Yamaki; T Gotoh
Journal:  Proc Natl Acad Sci U S A       Date:  1995-08-01       Impact factor: 11.205

3.  Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules.

Authors:  Selvaraj Muthukrishnan; Munish Puri
Journal:  BMC Res Notes       Date:  2018-05-11
  3 in total

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