Atomic resolution structure of concanavalin A at 120 K

Sean Parkin, Bernhard Rupp, Håkon Hope

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45 Scopus citations


The structure of native concanavalin A has been refined to a resolution of 1.2 Å against data collected at 120 K. The space group is I222, with a = 61.954(8), b = 86.053 (11), c = 89.079 (11) Å. The structure was refined by restrained weighted least squares minimization of Σw(F0/2-F1/2)2 with SHELXL92/3/6. The final model contains all of the atoms from 237 amino acids, two metal ions and 271 water molecules spread over 287 sites. Disorder is modelled over two conformations for 30 amino-acid side chains. The final weighted R index on F2 (wR2) on all data was 30.4%. Conventional R indices based on F were 14.2 and 11.8% for all data and for data with F>4σ(F), respectively.

Original languageEnglish
Pages (from-to)1161-1168
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6
StatePublished - 1996

ASJC Scopus subject areas

  • Structural Biology


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