Two-dimensional crystallization of catalase on a monolayer film of poly(1-benzyl-l-histidine) spread at the air/water interface

Ayano Sato, Taiji Furuno, Toyoshima Chikashi, Sasabe Hiroyuki

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Two-dimensional (2D) crystals of beef liver catalase were prepared by adsorption to a film of synthetic polypeptide, poly(1-benzyl-l-histidine) (PBLH), spread at the air/water interface. The crystallization experiments were carried out in the pH range of 4.8-6.4 for catalase solutions at low concentration (10 μg/ml). The pH-dependence suggested an electrostatic interaction in the binding of catalase to the PBLH film. At lower pH, small crystals were formed at a low binding rate, and at higher pH the binding was rapid and densely-packed 2D arrays with poor crystallinity were formed. To stimulate crystal growth, a thermal treatment was applied. One-shot heating of the interfacial catalase-PBLH film to 35-40°C was remarkably effective to form larger 2D crystals. The structure of catalase 2D crystals has been analyzed by Fourier filtering of the transmission electron micrographs. The crystal form is a new one, containing four catalase molecules in the unit cell with lattice parameters of a = 187 ○A, b = 225 ○A and γ = 92.8°.

Original languageEnglish
Pages (from-to)54-60
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number1-2
Publication statusPublished - 1993 Mar 5



  • Air/water interface
  • Annealing
  • Catalase
  • Monolayer
  • Poly(1-benzyl-L-histidine)
  • Two-dimensional crystal

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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