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

2.50
Hdl Handle:
http://hdl.handle.net/10547/228929
Title:
Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae.
Authors:
Meshcheryakov, Vladimir; Nitanai, Yasushi; Maytum, Robin; Geeves, Michael A.; Maeda, Yuichiro
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.
Affiliation:
ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c/o RIKEN Harima Institute SPring-8 Center, Sayo, Hyogo 679-5148, Japan. meshcher@spring8.or.jp
Citation:
Crystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae. 2008, 64 (Pt 6):528-530 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Issue Date:
1-Jun-2008
URI:
http://hdl.handle.net/10547/228929
DOI:
10.1107/S1744309108013110
PubMed ID:
18540067
Additional Links:
http://ukpmc.ac.uk/abstract/MED/18540067
Type:
Article
Language:
en
ISSN:
1744-3091
Appears in Collections:
Cell and Cryobiology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorMeshcheryakov, Vladimiren_GB
dc.contributor.authorNitanai, Yasushien_GB
dc.contributor.authorMaytum, Robinen_GB
dc.contributor.authorGeeves, Michael A.en_GB
dc.contributor.authorMaeda, Yuichiroen_GB
dc.date.accessioned2012-06-14T11:47:15Z-
dc.date.available2012-06-14T11:47:15Z-
dc.date.issued2008-06-01-
dc.identifier.citationCrystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae. 2008, 64 (Pt 6):528-530 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.en_GB
dc.identifier.issn1744-3091-
dc.identifier.pmid18540067-
dc.identifier.doi10.1107/S1744309108013110-
dc.identifier.urihttp://hdl.handle.net/10547/228929-
dc.description.abstractTropomyosin 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.en_GB
dc.language.isoenen
dc.relation.urlhttp://ukpmc.ac.uk/abstract/MED/18540067en_GB
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communicationsen_GB
dc.subject.meshAmino Acid Sequence-
dc.subject.meshBinding Sites-
dc.subject.meshCrystallization-
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshEscherichia coli-
dc.subject.meshHydrophobic and Hydrophilic Interactions-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshPliability-
dc.subject.meshProtein Isoforms-
dc.subject.meshRecombinant Proteins-
dc.subject.meshSaccharomyces cerevisiae-
dc.subject.meshSaccharomyces cerevisiae Proteins-
dc.subject.meshSerine-
dc.subject.meshTropomyosin-
dc.titleCrystallization and preliminary X-ray crystallographic analysis of full-length yeast tropomyosin 2 from Saccharomyces cerevisiae.en
dc.typeArticleen
dc.contributor.departmentERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c/o RIKEN Harima Institute SPring-8 Center, Sayo, Hyogo 679-5148, Japan. meshcher@spring8.or.jpen_GB
dc.identifier.journalActa crystallographica. Section F, Structural biology and crystallization communicationsen_GB

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