en
Scientific article
English

Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPΦ14-9 fusion protein

Published inFEBS letters, vol. 384, no. 3, p. 215-218
Publication date1996-04-22
First online date1999-11-30
Abstract

The SRPphi14-9 fusion protein, which can functionally replace the SRP9/14 heterodimer in the mammalian signal recognition particle (SRP), has been crystallized using the vapor diffusion method. Four different crystal forms were grown. SRPphi14-9 form IV crystals belong to the space group P4(1)22/ P4(3)22 with cell parameters a = b = 69.7 Angstroms, c = 95.7 Angstroms, alpha = beta = gamma = 90 degrees. A complete data set to 2.8 Angstroms resolution with an Rsym on intensities of 7.0% was collected on a single flash-frozen crystal.

eng
Keywords
  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Mammals
  • Molecular Sequence Data
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Selenomethionine / chemistry
  • Signal Recognition Particle / chemistry
  • Signal Recognition Particle / genetics
  • Recombinant Fusion Proteins
  • Signal Recognition Particle
  • Selenomethionine
Citation (ISO format)
BIRSE, Darcy E.A. et al. Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPΦ14-9 fusion protein. In: FEBS letters, 1996, vol. 384, n° 3, p. 215–218. doi: 10.1016/0014-5793(96)00315-8
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ISSN of the journal0014-5793
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