Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae.
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Japan Science and Technology AgencyIssue Date
2008-06-01
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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.Citation
Meshcheryakov, V., Nitanai, Y., Maytum, R., Geeves, M., Maeda, Y. (2008) 'Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae', Acta crystallographica. Section F, Structural biology and crystallization communications 64 (Pt 6):528-530PubMed ID
18540067Additional Links
http://ukpmc.ac.uk/abstract/MED/18540067Type
ArticleLanguage
enISSN
1744-3091ae974a485f413a2113503eed53cd6c53
10.1107/S1744309108013110
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