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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
384
Issue
3
Identifiers
DOI: 10.1016/0014-5793(96)00315-8
Keywords
  • Signal Recognition Particle (Srp)
  • Fusion Protein
  • Purification
  • Crystal
  • X-Ray Diffraction
  • Synchrotron
Disciplines
  • Biology

Abstract

Abstract The SRPΦ14-9 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. SRPΦ14-9 form IV crystals belong to the space group P4 122/P4 322 with cell parameters a = b = 69.7 A ̊ , c = 95.7 A ̊ , α = β = γ = 90° . A complete data set to 2.8 Å resolution with an R sym on intensities of 7.0% was collected on a single flashfrozen crystal.

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