Crystal structure of t4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli

D. R. Rose*, J. Phipps, J. Michniewicz, G. I. Birnbaum, F. R. Ahmed, A. Muir, W. F. Anderson, S. Narang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 Å resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.

Original languageEnglish (US)
Pages (from-to)277-282
Number of pages6
JournalProtein Engineering, Design and Selection
Volume2
Issue number4
DOIs
StatePublished - Oct 1988

Keywords

  • Protein X-ray crystallography
  • Protein folding
  • Synthetic gene

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Molecular Biology

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