• Publications
  • Influence
The crystal structure of EcoRV endonuclease and of its complexes with cognate and non‐cognate DNA fragments.
The structural results give new insight into the physical basis of the remarkable sequence specificity of this enzyme. Expand
A crystallographic study of metal-binding to yeast phenylalanine transfer RNA.
Different Fourier maps have revealed one major binding site for each of cobalt and managanese in the presence of magnesium, which is probably involved in the first stage of melting of the tRNA molecule, and may be critical for stabilizing the tertiary structure. Expand
Further refinement of the structure of yeast tRNAPhe.
The monoclinic crystal structure of yeast tRNA Phe is refined against a complete set of X-ray data at 2.5 A resolution, using real-space refinement and a combination of energy minimisation and crystallographic least-squares. Expand
Absence of substantial bending in Xenopus laevis transcription factor IIIA-DNA complexes.
Gel retardation of TFIIIA-DNA complexes with the I CR sequence contained in pBend3 indicates a bending angle of only 30 degrees and shows that interaction in the ICR could account for all of the bending found in the complete oocyte 5S RNA gene. Expand
Structure of yeast phenylalanine transfer RNA at 2.5 A resolution.
  • J. Ladner, A. Jack, +4 authors A. Klug
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1 November 1975
The x-ray analysis of the monoclinic form of yeast tRNAPhe has been taken to a resolution of 2.5 A by the method of isomorphous replacement and an extensive hydrogen bonding network is described involving specific interactions between bases and the ribose-phosphate backbone. Expand
Crystallographic and biochemical investigation of the lead(II)-catalyzed hydrolysis of yeast phenylalanine tRNA.
: X-ray diffraction data from monoclinic crystals of yeast tRNAPhe soaked in dilute lead(II) acetate solutions at pH 5.0 and at pH 7.4 have been collected to a resolution of 3 A, and the Pb(II)Expand
Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle.
Results indicate that one or more prolines undergo a structural rearrangement during the bR photocycle involving the Xaa-Pro C--N peptide bond, which may be directly coupled to the light-induced isomerization of the retinal chromophore from all-trans-retinal to 13-cis- retinal. Expand
Crystallization of pure species of bacterial tRNA for x-ray diffraction studies.
Crystallization conditions for both tR NATyr and tRNAPhe have been systematically investigated for a limited number of solvents and several forms of tRNATyr can be produced in a controlled fashion. Expand