Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

R Leberman

Showing results (61-70 of 76) with videos related to

Pageof 8
Sort By:
Nature|September 20, 1990
A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 AS Cusack, C Berthet-Colominas, M Härtlein, et al.
FEBS Letters|June 14, 1993
Crystallization of the seryl-tRNA synthetase:tRNAS(ser) complex of Escherichia coliS Price, S Cusack, F Borel, et al.
Nucleic Acids Research|April 11, 1995
Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylationC Vincent, F Borel, J C Willison, et al.
Nature|February 8, 1996
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolutionT Kawashima, C Berthet-Colominas, M Wulff, et al.
Journal of Molecular Biology|June 25, 1974
X-ray analysis of the disk of tobacco mosaic virus protein. I. Crystallization of the protein and of a heavy-atom derivativeR Leberman, J T Finch, P F Gilbert, et al.
Biophysical Chemistry|December 1, 1994
The triple isotopic substitution method in small angle neutron scattering. Application to the study of the ternary complex EF-Tu.GTP.aminoacyl-tRNAI N Serdyuk, Pavlov MYu, I N Rublevskaya, et al.
Nature|June 1, 1989
Neutron scatteringS Cusack, B Jacrot, R Leberman, et al.
Biochemical and Biophysical Research Communications|March 13, 1986
31P-NMR spectra of the Ha-ras p21.nucleotide complexesP Rösch, A Wittinghofer, J Tucker, et al.
Analytical Biochemistry|May 1, 1980
A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-TuR Leberman, B Antonsson, R Giovanelli, et al.
The EMBO Journal|June 10, 1998
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acidC Berthet-Colominas, L Seignovert, M Härtlein, et al.
Pageof 8

Showing results (61-70 of 76) with videos related to

Sort By:
Pageof 8
Nature|September 20, 1990
A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 AS Cusack, C Berthet-Colominas, M Härtlein, et al.
FEBS Letters|June 14, 1993
Crystallization of the seryl-tRNA synthetase:tRNAS(ser) complex of Escherichia coliS Price, S Cusack, F Borel, et al.
Nucleic Acids Research|April 11, 1995
Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylationC Vincent, F Borel, J C Willison, et al.
Nature|February 8, 1996
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolutionT Kawashima, C Berthet-Colominas, M Wulff, et al.
Journal of Molecular Biology|June 25, 1974
X-ray analysis of the disk of tobacco mosaic virus protein. I. Crystallization of the protein and of a heavy-atom derivativeR Leberman, J T Finch, P F Gilbert, et al.
Biophysical Chemistry|December 1, 1994
The triple isotopic substitution method in small angle neutron scattering. Application to the study of the ternary complex EF-Tu.GTP.aminoacyl-tRNAI N Serdyuk, Pavlov MYu, I N Rublevskaya, et al.
Nature|June 1, 1989
Neutron scatteringS Cusack, B Jacrot, R Leberman, et al.
Biochemical and Biophysical Research Communications|March 13, 1986
31P-NMR spectra of the Ha-ras p21.nucleotide complexesP Rösch, A Wittinghofer, J Tucker, et al.
Analytical Biochemistry|May 1, 1980
A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-TuR Leberman, B Antonsson, R Giovanelli, et al.
The EMBO Journal|June 10, 1998
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acidC Berthet-Colominas, L Seignovert, M Härtlein, et al.
Pageof 8