Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Siegfried Lorenz"'
Autor:
Volker A. Erdmann, M. Perbandt, Corinna Lippmann, L.J. DeLucas, Karen M. Moore, Ch. Betzel, Siegfried Lorenz
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 56:498-500
Thermus flavus 5S rRNA with a molecular weight of about 40 kDa was modified at the 5' and 3' ends. Crystals were obtained under earth and microgravity conditions. The best crystals were obtained during NASA space mission STS 94. For the first time, i
Autor:
Keith S. Wilson, Volker A. Erdmann, Zbigniew Dauter, Elke Raderschall, Siegfried Lorenz, Christian Betzel
Publikováno v:
Journal of Molecular Biology. 219:399-402
Crystals of purified 5 S rRNA from Thermus flavus have been obtained. The crystals diffract up to 8 A resolution, using synchrotron radiation, and have the monoclinic space-group C2 . The unit cell has the dimensions a = 190 A , b = 110 A , c = 138 A
Publikováno v:
BIOmaterialien. 2
Publikováno v:
RNA Biochemistry and Biotechnology ISBN: 9780792358626
The ribosomal 5S RNA is approximately 120 nucleotides long and is an integral part of the large ribosomal subunit. Several parts of the 5S rRNA interact specifically with several ribosomal proteins [1–3]. Nevertheless its precise role in protein sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::16e7723ee10117d6fb3c632b3f537773
https://doi.org/10.1007/978-94-011-4485-8_4
https://doi.org/10.1007/978-94-011-4485-8_4
Autor:
M. B. Garber, Volker A. Erdmann, Siegfried Lorenz, Anders Liljas, G.M. Gongadze, Werner Schroeder, I.A Kashparov
Publikováno v:
FEBS letters. 386(2-3)
An unusual acidic ribosomal protein from Thermus thermophilus, TL5, that binds to 5S rRNA specifically and strongly, has been investigated. The N-terminal sequence of TL5 does not reveal any homology with known ribosomal proteins. Two large tryptic f
Autor:
Volker A. Erdmann, J.P. Fürste, Keith S. Wilson, Rolf Bald, Siegfried Lorenz, Th.R. Schneider, M. Zhang, Ch. Betzel
Publikováno v:
FEBS letters. 351(2)
This is the first high resolution crystal structure of an RNA molecule made by solid phase chemical synthesis and representing a natural RNA. The structure of the domain A of Thermus flavus ribosomal 5S RNA is refined to R = 18% at 2.4 Å including 1
Autor:
Keith S. Wilson, Ch. Betzel, Volker A. Erdmann, Siegfried Lorenz, Jens P. Fürste, E. Raderschall, Z. Dauter, M. Zhang, Rolf Bald
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 49(Pt 4)
Crystals of domain A of Thermus flavus 5S rRNA have been obtained. The space group was found to be P4(3) with unit-cell dimensions a = b = 30.10 and c = 86.80 A. Data to 2.3 A have been recorded and solution of the structure is currently underway by
Autor:
Siegfried Lorenz, Volker A. Erdmann, J.P. Fürste, Keith S. Wilson, E. Raderschall, Ch. Betzel, Rolf Bald, M. Zhang
Publikováno v:
The Translational Apparatus ISBN: 9781461360216
Although it has been established that the ribosomal 5S RNA is essential for the biological function of the ribosomes (Nomura and Erdmann, 1970; Erdmann et al., 1971 a, b; Nierhaus and Dohme, 1974; Dohme and Nierhaus, 1976; Hartmann et al., 1988), its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b97e11a99d26e2de9cc9d32ad36f6177
https://doi.org/10.1007/978-1-4615-2407-6_47
https://doi.org/10.1007/978-1-4615-2407-6_47
Publikováno v:
European journal of biochemistry. 204(2)
Different stable forms of Escherichia coli and rat liver 5S rRNA have been probed by Pb(II)-induced hydrolysis. In the native A forms of 5S rRNA, Pb2+ reveal single-stranded RNA stretches and regions of increased conformational flexibility or distort