Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form

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Abstract

The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 Å and c = 276.7 Å with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 Å consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement.

Original languageEnglish
Pages (from-to)283-286
Number of pages4
JournalProteins: Structure, Function and Bioinformatics
Volume20
Issue number3
DOIs
Publication statusPublished - 1994

Fingerprint

Rhodospirillaceae
Rhodobacter sphaeroides
Heptanes
Crystallization
Detergents
Amphiphiles
Crystals
Proteins
Diffraction
benzamidine
polyethylene glycol 4000
Datasets
octyl-beta-D-glucoside

Keywords

  • detergent
  • membrane protein
  • photosynthesis
  • pigment- protein complexes
  • protein structure

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

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abstract = "The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 {\AA} and c = 276.7 {\AA} with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 {\AA} consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5{\%}. Analysis of the diffraction data is underway using molecular and isomorphous replacement.",
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AB - The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 Å and c = 276.7 Å with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 Å consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement.

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KW - protein structure

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