Crystallization and preliminary diffraction studies of a human Fabμ with anti-I activity

A. Cauerhff, I. Polikarpov, I. Mathov, C. Abatangelo, L. Plotkin, F. A. Goldbaum, J. Leoni

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Abstract

An Fabμ from a human monoclonal cold agglutinin (KAU) was obtained by tryptic digestion and purified to homogeneity by FPLC. Crystals were grown by hanging drop vapour diffusion technique against mother liquor containing Sodium Hepes pH 7.5, and PEG 8000 as precipitant. Crystals were found to belong to the trigonal space group P3121(P3221) with the cell parameters a=b=114.233 Å, c=172.787 Å. The crystals diffracted at least to 2.8 Å resolution at a synchrotron beamline.

Original languageEnglish (US)
Pages (from-to)177-180
Number of pages4
JournalProtein and Peptide Letters
Volume5
Issue number3
StatePublished - Dec 1 1998

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ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

Cauerhff, A., Polikarpov, I., Mathov, I., Abatangelo, C., Plotkin, L., Goldbaum, F. A., & Leoni, J. (1998). Crystallization and preliminary diffraction studies of a human Fabμ with anti-I activity. Protein and Peptide Letters, 5(3), 177-180.