By the same authors

From the same journal

Crystallization and preliminary X-ray crystallographic studies of the plant aspartic proteinase cardosin A

Research output: Contribution to journalArticle


  • I Bento
  • C Frazao
  • R Coelho
  • K Wilson
  • Z Dauter
  • M A Carrondo


Publication details

JournalActa Crystallographica Section D: Biological Crystallography
DatePublished - 1 Sep 1998
Number of pages3
Pages (from-to)991-993
Original languageEnglish


The plant aspartic proteinase cardosin A was crystallized using vapour diffusion. Crystals belong to the monoclinic space group C2, cell dimensions a = 116.9(2), b = 87.2(8), c = 81.3 (1) Angstrom, beta = 104.4 (4)degrees, and contain two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Diffraction data were collected at room temperature with radiation from a synchrotron source up to 2.85 Angstrom resolution. When the crystals were flash cooled to 110 K in a nitrogen stream the same resolution limit could also be obtained on a rotating-anode source. Recently, synchrotron radiation together with hash cooling led to an improvement of the diffraction data to 1.72 Angstrom resolution.

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations