Meshcheryakov, V. and Nitanai, Y. and Maytum, R. and Geeves, M.A. and Maeda, Y. (2008) Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae. Acta Crystallogr Section F-Structural Biology and Crystallization Communications, 64 (Pt 6). pp. 528-530. ISSN 1744-3091 .
|The full text of this publication is not available from this repository. (Contact us about this Publication)|
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.
|Additional information:||Journal Article Research Support, Non-U.S. Gov't England|
|Uncontrolled keywords:||Amino Acid Sequence Binding Sites Crystallization Crystallography, X-Ray Escherichia coli/genetics Hydrophobicity Molecular Sequence Data Pliability Protein Isoforms/chemistry/genetics Recombinant Proteins/chemistry Saccharomyces cerevisiae/*chemistry/genetics Saccharomyces cerevisiae Proteins/*chemistry/genetics Serine/chemistry Tropomyosin/*chemistry/genetics|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Michael Geeves|
|Date Deposited:||15 May 2009 10:24|
|Last Modified:||15 May 2009 10:24|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/13222 (The current URI for this page, for reference purposes)|
- Depositors only (login required):