Crystallization and preliminary crystallographic studies of an antimicrobial protein from Pharbitis nil

Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):263-5. doi: 10.1107/s090744490001516x.

Abstract

An antimicrobial protein from seeds of Pharbitis nil (Pn-AMP) which shows an antifungal activity towards several agriculturally important plant pathogens has been crystallized in the presence of equimolar N-acetylglucosamine with sodium citrate as precipitant. The crystal belongs to the hexagonal space group P6(1)22 (or P6(5)22), with unit-cell parameters a = b = 29.33 (5), c = 133.44 (12) A. Native data were collected using a crystal at 100 K to a resolution of 1.78 A.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / isolation & purification
  • Antifungal Agents / chemistry
  • Crystallization
  • Crystallography, X-Ray
  • Magnoliopsida / chemistry*
  • Molecular Sequence Data
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Seeds / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Anti-Infective Agents
  • Antifungal Agents
  • Plant Proteins