Refined structure of the chitinase from barley seeds at 2.0 a resolution.

@article{Song1996RefinedSO,
  title={Refined structure of the chitinase from barley seeds at 2.0 a resolution.},
  author={Hyun Kyu Song and Se Won Suh},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={1996},
  volume={52 Pt 2},
  pages={289-98}
}
Chitinase from barley seeds is a monomeric enzyme with 243 amino-acid residues and it plays a role as a defense protein. Its structure, previously determined at 2.8 A resolution by multiple isomorphous replacement method, is mainly alpha-helical [Hart, Monzingo, Ready, Ernst & Robertus, (1993). J. Mol. Biol. 229, 189-193]. The crystallization and preliminary X-ray data of the same enzyme in a different crystal form has been reported independently [Song, Hwang, Kim & Suh, (1993). Proteins, 17… CONTINUE READING