Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds

Hyun Kyu Song, Se Won Suh

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Bowman-Birk trypsin inhibitor from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is tetragonal, belonging to the space group P41212 (or P43212), with unit-cell parameters of a = b = 62.48 and c = 94.63 Å. The asymmetric unit contains one molecule of Bowman-Birk trypsin inhibitor with corresponding crystal volume per protein mass (V(m)) of 2.89 Å3 Da-1 and the solvent content of 57% by volume. The crystals diffract to at least 1.9 Å Bragg spacing upon exposure to synchrotron X-rays. X-ray data to 1.9 Å have been collected from a native crystal.

Original languageEnglish
Pages (from-to)441-443
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number3
DOIs
Publication statusPublished - 1998 May 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds'. Together they form a unique fingerprint.

  • Cite this