Purification, crystallization and preliminary X-ray diffraction studies of recombinant calcium-binding domain of the small subunit of porcine calpain

Academic Article

Abstract

  • The calcium-binding domain of the small subunit of porcine calpain (domain VI) has been expressed in Escherichia coli, purified, and crystallized in the presence of Ca2+. Two crystal forms have been obtained by the vapor-diffusion method using PEG 6000 as the precipitant. Crystal form I, belonging to trigonal space group P3121 (or P3221) with cell dimensions a = b = 79.8, c = 57.08 Å, α = β = 90.0 and γ = 120.0°diffracted to 2.8 Å. The second crystal form diffracts to 1.8 Å and belongs to monoclinic space group P21 with cell dimensions a = 50.1, b = 79.7, c = 57.1 Å and β = 91.2°.
  • Digital Object Identifier (doi)

    Author List

  • Lin GD; Chattopadhyay D; Maki M; Takano E; Hatanaka M; Delucas L; Narayana SVL
  • Start Page

  • 474
  • End Page

  • 476
  • Volume

  • 53
  • Issue

  • 4