A mannose-specific agglutinin from garlic (Allium sativum) which forms part of a well conserved super-family of bulb lectins has been purified and crystallized by the hanging-drop vapour-diffusion technique, by equilibrating with a 20% solution of PEG 8000 in the presence of alpha-D-mannose. Crystals of the dimeric form of this protein are monoclinic C2 with unit-cell dimensions a = 203.2, b = 43.8, c = 79.3 A and beta = 112.4 degrees and have two dimers in the asymmetric unit. Data have been collected to 2.4 A resolution and the structure solved by molecular replacement using the coordinates of the snowdrop lectin as the search model.

DOI: 10.1107/S0907444997007385
Version: za2963e q8zae q8zbd q8zcf q8zdd q8ze1 q8zfb q8zge