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Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae.

Research Output: Contribution to journal Article Peer-review

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Abstract

Tropomyosin is a highly conserved actin-binding protein that is found in most eukaryotic cells. It is critical for actin-filament stabilization and for cooperative regulation of many actin functions. Detailed structural information on tropomyosin is very important in order to understand the mechanisms of its action. Whereas structures of isolated tropomyosin fragments have been obtained at high resolution, the atomic structure of the entire tropomyosin molecule is still unknown. Here, the crystallization and preliminary crystallographic analysis of full-length yeast tropomyosin 2 (yTm2) from Saccharomyces cerevisiae are reported. Recombinant yTm2 expressed in Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group C2, with unit-cell parameters a = 154.8, b = 49.9, c = 104.0 A, alpha = gamma = 90.0, beta = 124.0 degrees and two molecules in the asymmetric unit. A complete native X-ray diffraction data set was collected to 3.5 A resolution using synchrotron radiation.

Publication Information

Output type

Research Output: Contribution to journal Article Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 528-530

Journal (Volume, Issue Number)

Acta Crystallographica Section F: Structural Biology and Crystallization Communications (Volume 64, Issue Pt 6)

Publication milestones

  • Published - 01/06/2008

Publication status

Published - 01/06/2008

External Publication IDs

  • handle.net: 10547/228929
  • Scopus: 46249121084

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