Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds

Kyu Song Hyun Kyu Song, Yeon Hwang Kwang Yeon Hwang, Kyu Kim Kyeong Kyu Kim, Won Suh Se Won Suh

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P21, with unit cell parameters of a = 69.43 Å, b = 44.55 Å, c = 81.41 Å, and β = 111.95°. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (V(M)) of 2.25 Å3/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 Å with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 Å Bragg spacing from a native crystal.

Original languageEnglish
Pages (from-to)107-109
Number of pages3
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - 1993
Externally publishedYes


  • X-ray diffraction
  • antifungal protein
  • crystals
  • plant chitinase

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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