Literature DB >> 6427471

Preliminary X-ray diffraction study of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum.

G Schneider, C I Brändén, G Lorimer.   

Abstract

Crystals from the dimeric enzyme ribulose-1,5-bisphosphate carboxylase of the photosynthetic bacterium Rhodospirillum rubrum have been obtained from the gene product expressed in Escherichia coli. The crystals are of the quarternary complex comprising enzyme: activator CO2 (as a carbamate): Mg2+: 2- carboxyarabinitol -1,5-bisphosphate (as a transition state analog). X-ray diffraction photographs show symmetry consistent with space group P4(1)2(1)2 or the corresponding enantiomorphic space group. Cell parameters are a = b = 82 A, c = 324 A with two subunits per asymmetric unit. The crystals diffract to at least 3 A resolution.

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Year:  1984        PMID: 6427471     DOI: 10.1016/0022-2836(84)90450-9

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


  2 in total

1.  Structure of glycolate oxidase from spinach.

Authors:  Y Lindqvist; C I Brändén
Journal:  Proc Natl Acad Sci U S A       Date:  1985-10       Impact factor: 11.205

2.  A site-specific mutation within the active site of ribulose-1,5-bisphosphate carboxylase of Rhodospirillum rubrum.

Authors:  S Gutteridge; I Sigal; B Thomas; R Arentzen; A Cordova; G Lorimer
Journal:  EMBO J       Date:  1984-12-01       Impact factor: 11.598

  2 in total

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