Crystallization and preliminary X-ray crystallographic analysis of the α-2,6-sialyltransferase PM0188 from Pasteurella multosida

Dong Uk Kim, Ji Ho Yoo, Kang Ryu, Hyun Soo Cho

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Sialyltransferase is an enzyme that transfers the sialic acid moiety from cytidine-5-monophospho-N-acetylneuraminic acid (CMP-NeuAc) to the carbohydrate group of various glycoproteins. These glycoproteins are involved in inflammation, embryogenesis, immune defence and metastasis of cancer cells by cell-cell interactions or cell-matrix interactions. The α-2,6- sialyltransferase PM0188 from Pasteurella multocida was purified using affinity-column chromatographic methods and crystallized using the hanging-drop vapour-diffusion method at 293 K. MAD data were collected to 1.9 Å resolution from an SeMet-substituted crystal. The crystal belongs to space group P21, with unit-cell parameters a = 52.9, b = 61.0, c = 64.6 Å, α = γ = 90, β = 112.3°. Assuming the presence of one molecule in the asymmetric unit, the solvent content is estimated to be about 45%.

Original languageEnglish
Pages (from-to)142-144
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number2
DOIs
Publication statusPublished - 2006 Feb 1

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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