Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded ω transcriptional repressor

Kazutaka Murayama, Ana B. De La Hoz, Claudia Alings, Gema López, Peter Orth, Juan C. Alonso, Wolfram Saenger

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The transcriptional repressor, ω protein, from the Streptococcus pyogenes broad-host-range plasmid pSM19035 was crystallized at pH 7.5 and 8.5 by the vapour-diffusion method using PEG 4000 as precipitant. Two crystal forms were obtained; the first belongs to the tetragonal space group P41212 or P43212 and the second to the hexagonal space group P61 or P65. The crystals are most likely to contain one ω protein in the asymmetric unit, with V(m) values of 3.2 and 3.5 Å3 Da-1, respectively. The crystals diffract X-rays to 2.4 and 2.9 Å resolution for the tetragonal and hexagonal systems, respectively.

Original languageEnglish
Pages (from-to)2041-2042
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number12
DOIs
Publication statusPublished - 1999 Dec 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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