Crystallization and preliminary X-ray analysis of a complex between the Bowman-Birk trypsin inhibitor from barley and porcine pancreatic trypsin

Young Sil Kim, Hyun Kyu Song, Se Won Suh

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A 1:2 complex between the Bowman-Birk trypsin inhibitor from barley seeds and porcine pancreatic trypsin has been crystallized at 291 K using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.10, b = 88.38 and c = 203.65 Å. The asymmetric unit contains two monomers of the complex, with a corresponding V(m) of 2.41 293 Da-1 and a solvent content of 49%. Native data to 2.2 Å resolution have been collected at 100 K using synchrotron X-rays.

Original languageEnglish
Pages (from-to)1244-1246
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number6
DOIs
Publication statusPublished - 1999 Jun 1
Externally publishedYes

Fingerprint

barley
trypsin
Synchrotrons
Trypsin Inhibitors
X ray analysis
Hordeum
Crystallization
Trypsin
inhibitors
Seed
Seeds
Swine
Monomers
X-Rays
crystallization
X rays
Crystals
glycols
polyethylenes
seeds

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

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abstract = "A 1:2 complex between the Bowman-Birk trypsin inhibitor from barley seeds and porcine pancreatic trypsin has been crystallized at 291 K using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.10, b = 88.38 and c = 203.65 {\AA}. The asymmetric unit contains two monomers of the complex, with a corresponding V(m) of 2.41 293 Da-1 and a solvent content of 49{\%}. Native data to 2.2 {\AA} resolution have been collected at 100 K using synchrotron X-rays.",
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T1 - Crystallization and preliminary X-ray analysis of a complex between the Bowman-Birk trypsin inhibitor from barley and porcine pancreatic trypsin

AU - Kim, Young Sil

AU - Song, Hyun Kyu

AU - Suh, Se Won

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Y1 - 1999/6/1

N2 - A 1:2 complex between the Bowman-Birk trypsin inhibitor from barley seeds and porcine pancreatic trypsin has been crystallized at 291 K using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.10, b = 88.38 and c = 203.65 Å. The asymmetric unit contains two monomers of the complex, with a corresponding V(m) of 2.41 293 Da-1 and a solvent content of 49%. Native data to 2.2 Å resolution have been collected at 100 K using synchrotron X-rays.

AB - A 1:2 complex between the Bowman-Birk trypsin inhibitor from barley seeds and porcine pancreatic trypsin has been crystallized at 291 K using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.10, b = 88.38 and c = 203.65 Å. The asymmetric unit contains two monomers of the complex, with a corresponding V(m) of 2.41 293 Da-1 and a solvent content of 49%. Native data to 2.2 Å resolution have been collected at 100 K using synchrotron X-rays.

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