title: Two crystal forms of the lentil lectin diffract to high resolution.
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.
authors.affiliation: Laboratorium voor ultrastructuur, Vrije Universiteit Brussel, Belgium.
authors.forename: R
authors.initials: R
authors.lastname: Loris
authors.forename: J
authors.initials: J
authors.lastname: Lisgarten
authors.forename: D
authors.initials: D
authors.lastname: Maes
authors.forename: R
authors.initials: R
authors.lastname: Pickersgill
authors.forename: F
authors.initials: F
authors.lastname: Körber
authors.forename: C
authors.initials: C
authors.lastname: Reynolds
authors.forename: L
authors.initials: L
authors.lastname: Wyns
mesh_terms: D003461:Crystallography; D037102:Lectins / Q000737:chemistry*; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; C033619:lentil lectin