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  • Title: Crystallization and preliminary X-ray diffraction analysis of the seed lectin from Parkia platycephala.
    Author: Gallego del Sol F, Ramón-Maiques S, Santos CF, Grangeiro TB, Nagano CS, Farias CM, Cavada BS, Calvete JJ.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Jan; 58(Pt 1):167-9. PubMed ID: 11752802.
    Abstract:
    The crystallization and preliminary X-ray diffraction analysis of the seed lectin of Parkia platycephala, a Mimosoideae, regarded as the most primitive group of the Leguminosae plants, are reported. Its amino-acid sequence consists of three tandemly arranged jacalin-related beta-prism domains, which is a novel fold for a leguminous lectin. Furthermore, no other lectin structure with this arrangement of domains has been described. P2(1)2(1)2(1) crystals (unit-cell parameters a = 63.6, b = 68.5, c = 208.5 A), which diffract to a maximum resolution of 2.2 A, were obtained in hanging drops at pH 8 and 293 K by the vapor-diffusion method using 10% 2-propanol and 20% polyethylene glycol 4000 as precipitants. The asymmetric unit contains two lectin molecules and has a solvent content of 46%. Only a single beta-prism domain could be located by molecular replacement using the structure of the Helianthus tuberosus lectin (PDB code 1c3k) as the search model. Isomorphous heavy-atom derivatives are currently being produced to solve the complete structure of the P. platycephala seed lectin.
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