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

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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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
Volume17
Issue number1
Publication statusPublished - 1993 Jan 1
Externally publishedYes

Fingerprint

Chitinases
Hordeum
Crystallization
Seed
Seeds
X-Rays
X rays
Crystals
Electrodes
Anodes
Temperature
Molecules
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology

Cite this

Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds. / Song, Hyun Kyu; Hwang, Kwang Yeon; Kyeong Kyu Kim, Kyu Kim; Se Won Suh, Won Suh.

In: Proteins: Structure, Function and Genetics, Vol. 17, No. 1, 01.01.1993, p. 107-109.

Research output: Contribution to journalArticle

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