Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds

Kwang Yeon Hwang, Kyeong Kyu Kim, Kyeongsik Min, Soo Hyun Eom, Yeon Gyu Yu, Sangsoo Kim, Robert M. Sweet, Se Won Suh

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 Å upon exposure to synchrotron X-rays. The crystals belong to the space group P41212 (or P43212) with unit cell dimensions of a = 38.02 Å and c = 98.98 Å. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 Å3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 Å Bragg spacing from native crystals.

Original languageEnglish
Pages (from-to)255-257
Number of pages3
JournalJournal of Molecular Biology
Volume229
Issue number1
Publication statusPublished - 1993 Dec 1
Externally publishedYes

Keywords

  • Crystallization
  • Phospholipid transfer protein
  • Possible amylase/protease inhibitor
  • Preliminary X-ray analysis
  • Rice seeds

ASJC Scopus subject areas

  • Virology

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  • Cite this

    Hwang, K. Y., Kim, K. K., Min, K., Eom, S. H., Yu, Y. G., Kim, S., Sweet, R. M., & Suh, S. W. (1993). Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds. Journal of Molecular Biology, 229(1), 255-257.