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The Structure of the Pea Lectin-D-mannopyranose Complex at a 2.1 Å Resolution

  • S. N. Ruzheinikov
  • , I. Yu Mikhailova
  • , I. N. Tsygannik
  • , W. Pangborn
  • , W. Duax
  • , V. Z. Pletnev
  • Russian Academy of Sciences
  • Hauptman Woodward Medical Institute

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The structure of a new crystal complex (P212121 spatial group, cell dimensions: a 73.926, b 104.083, and c 64.837 Å) of pea lectin (Pisum sativum, dimer, molecular mass ca. 52 kDa) with D-mannopyranose was established by the molecular replacement approach at a resolution of 2.1 Å. After crystallographic refinement, the value of the R-factor was 16.1%. The mannose molecule was shown to be fixed by six hydrogen bonds with Asp81, Gly99, Asn125, Ala217, and Glu218.

Original languageEnglish
Pages (from-to)315
Number of pages1
JournalBioorganicheskaya Khimiya
Volume24
Issue number4
StatePublished - Apr 1998

Keywords

  • Crystal complex
  • Pea lectin
  • X-ray analysis

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