Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea

Research output: Contribution to journal › Journal article › Research › peer-review

  • L K Skov
  • Osman Asghar Mirza
  • A Henriksen
  • G Potocki de Montalk
  • M Remaud-Simeon
  • P Sarcabal
  • R M Willemot
  • P Monsan
  • Gajhede, Michael
Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
Original languageEnglish
JournalActa Crystallographica. Section D: Biological Crystallography
Volume56
Issue numberPt 2
Pages (from-to)203-5
Number of pages3
ISSN0907-4449
Publication statusPublished - Feb 2000
Externally publishedYes

    Research areas

  • Bacterial Proteins, Circular Dichroism, Crystallization, Crystallography, X-Ray, Escherichia coli, Glucosyltransferases, Neisseria, Recombinant Proteins

ID: 47295081