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

Authors
  • Loris, R
  • Lisgarten, J
  • Maes, D
  • Pickersgill, R
  • Körber, F
  • Reynolds, C
  • Wyns, L
Type
Published Article
Journal
Journal of molecular biology
Publication Date
Jan 20, 1992
Volume
223
Issue
2
Pages
579–581
Identifiers
PMID: 1738165
Source
Medline
License
Unknown

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.

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