Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

Paul M. Horowitz, Kuldeep Patel

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The activity and crystal stability of the enzyme thiosulfate sulfurtransferase were studied as a function of ionic strength. At 2 M ammonium sulfate, where the x-ray structural studies of this protein were done soluble enzyme has low activity (<16% of the activity of the enzyme at an ionic strength of 0.1) and crystals of the enzyme are stable when substrates are added. However, at 1.4 M ammonium sulfate, crystals of TST rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O3=. These results are consistent with a conformational change on converting the sulfur substituted form of the enzyme (ES) to the sulfur-free form (E) and helps to explain why this change was not observed in the crystallographic studies.

Original languageEnglish (US)
Pages (from-to)419-423
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - May 30 1980
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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