Literature DB >> 2995685

Crystallization and preliminary diffraction data for iso-1-cytochrome c from yeast.

C Sherwood, G D Brayer.   

Abstract

Deep red crystals of the electron transfer protein, iso-1-cytochrome c from yeast (Saccharomyces cerevisiae), have been obtained from a 90% saturated solution of (NH4)2SO4 containing 2 mg protein/ml, 0.1 M-sodium phosphate and adjusted to pH 6.7. The space group is P4(1)2(1)2 (or P4(3)2(1)2) with a = b = 36.4 A, c = 136.8 A and Z = 8. Crystals are stable for at least ten days in the X-ray beam and diffract to better than 2.0 A resolution. Comparable and morphologically similar crystal forms of three iso-1-cytochrome c mutants at Phe87, a pivotal residue in the electron transport chain, have also been obtained.

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Year:  1985        PMID: 2995685     DOI: 10.1016/0022-2836(85)90192-5

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


  1 in total

1.  Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.

Authors:  T P Lo; M E Murphy; J G Guillemette; M Smith; G D Brayer
Journal:  Protein Sci       Date:  1995-02       Impact factor: 6.725

  1 in total

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