Open AccessCrystallization and preliminary X‐ray crystallographic analysis of full‐length yeast tropomyosin 2 from Saccharomyces cerevisiae
Author(s) -
Meshcheryakov Vladimir,
Nitanai Yasushi,
Maytum Robin,
Geeves Michael A.,
Maeda Yuichiro
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108013110
Subject(s) - tropomyosin , saccharomyces cerevisiae , fiber diffraction , crystallography , actin , crystallization , yeast , escherichia coli , protein filament , chemistry , x ray crystallography , myosin , resolution (logic) , recombinant dna , diffraction , biochemistry , physics , optics , organic chemistry , gene , artificial intelligence , computer science
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 C 2, with unit‐cell parameters a = 154.8, b = 49.9, c = 104.0 Å, α = γ = 90.0, β = 124.0° and two molecules in the asymmetric unit. A complete native X‐ray diffraction data set was collected to 3.5 Å resolution using synchrotron radiation.