Crystallization and preliminary X-ray diffraction studies of dialkylglycine decarboxylase, a decarboxylating transaminase

Michael D. Toney, John W. Keller, Richard A. Pauptit, Joachim Jaeger, Matthew K. Wise, Ursula Sauder, Johan N. Jansonius

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

The pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase (E.C. 4.1.1.64) has been crystallized by vapor diffusion from a 15% polyethyleneglycol solution with sodium pyruvate as coprecipitant. The space group of the crystals is either P6222 or the enantiomorph, P6422, with one subunit of 46,500 Da per asymmetric unit. The unit cell has dimensions a = b = 152·7 A ̊, c = 86·6 A ̊, α = β = 90 °, γ = 120 °, and a solvent content of approximately 61%. Diffraction extends to 2·3 Å resolution.

Original languageEnglish (US)
Pages (from-to)873-875
Number of pages3
JournalJournal of Molecular Biology
Volume222
Issue number4
DOIs
StatePublished - Dec 20 1991
Externally publishedYes

Keywords

  • crystallization
  • decarboxylation
  • transamination
  • vitamin B
  • X-ray crystallography

ASJC Scopus subject areas

  • Virology

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    Toney, M. D., Keller, J. W., Pauptit, R. A., Jaeger, J., Wise, M. K., Sauder, U., & Jansonius, J. N. (1991). Crystallization and preliminary X-ray diffraction studies of dialkylglycine decarboxylase, a decarboxylating transaminase. Journal of Molecular Biology, 222(4), 873-875. https://doi.org/10.1016/0022-2836(91)90580-Y