Two crystal forms of the lentil lectin diffract to high resolution.

TitleTwo crystal forms of the lentil lectin diffract to high resolution.
Publication TypeJournal Article
Year of Publication1992
AuthorsLoris, R., J. Lisgarten, D. Maes, R. Pickersgill, F. K├Ârber, C. Reynolds, and L. Wyns
JournalJ Mol Biol
Volume223
Issue2
Pagination579-81
Date Published1992 Jan 20
ISSN0022-2836
KeywordsCrystallography, 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 JournalJ. Mol. Biol.
PubMed ID1738165