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.
|Number of pages||8|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - 1996|
ASJC Scopus subject areas
- Structural Biology