Title | Two crystal forms of the lentil lectin diffract to high resolution. |
Publication Type | Journal Article |
Year of Publication | 1992 |
Authors | Loris, R., J. Lisgarten, D. Maes, R. Pickersgill, F. Körber, C. Reynolds, and L. Wyns |
Journal | J Mol Biol |
Volume | 223 |
Issue | 2 |
Pagination | 579-81 |
Date Published | 1992 Jan 20 |
ISSN | 0022-2836 |
Keywords | Crystallography, Lectins, Plant Lectins, Plant Proteins, Protein Conformation |
Abstract | The legume lectins are an important class of polysaccharide-binding proteins with a wide range of biochemical and immunological applications. Two high-resolution crystal forms are obtained for the lentil (Lens culinaris) lectin: a monoclinic P21 and an orthorhombic P212121. The unit cell dimensions for the monoclinic form are a = 58.0 A, b = 56.0 A, c = 82.1 A, beta = 104.4 degrees, while for the orthorhombic form a = 56.4 A, b = 74.6 A, c = 124.9 A. The asymmetric unit contains one dimer in both cases. The crystals diffract to 1.7 A resolution using synchrotron radiation. Preliminary data have been collected to 2.3 A on both crystal forms using a conventional X-ray source. |
Alternate Journal | J. Mol. Biol. |
PubMed ID | 1738165 |
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