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