Cloning, expression, crystallization and preliminary X-ray data analysis of norcoclaurine synthase from Thalictrum flavum

Alessandra Pasquo, Alessandra Bonamore, Stefano Franceschini, Alberto Macone, Alberto Boffi, Andrea Ilari

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19 Citations (Scopus)


Norcoclaurine synthase (NCS) catalyzes the condensation of 3,4-dihydroxy-phenylethylamine (dopamine) and 4-hydroxyphenylacetaldehyde (4-HPAA) as the first committed step in the biosynthesis of benzylisoquinoline alkaloids in plants. The protein was cloned, expressed and purified. Crystals were obtained at 294 K by the hanging-drop vapour-diffusion method using ammonium sulfate and sodium chloride as precipitant agents and diffract to better than 3.0 Å resolution using a synchrotron-radiation source. The crystals belong to the trigonal space group P3121, with unit-cell parameters a = b = 86.31, c = 118.36 Å. A selenomethionine derivative was overexpressed, purified and crystallized in the same space group. A complete MAD data set was collected at 2.7 Å resolution. The model is under construction. © International Union of Crystallography 2008.
Original languageEnglish
Pages (from-to)281 - 283
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number4
Publication statusPublished - 29 Mar 2008
Externally publishedYes


All Science Journal Classification (ASJC) codes

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

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