Restrained least-squares refinement of the crystal structure of the ribonuclease T1*2'-guanylic acid complex at 1·9 Å resolution
- 1 December 1987
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica Section B, Structural science, crystal engineering and materials
- Vol. 43 (6), 548-554
- https://doi.org/10.1107/s0108768187097337
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Inquiries into the structure-function relationship of ribonuclease T1 using chemically synthesized coding sequences.Proceedings of the National Academy of Sciences, 1986
- A Revision and Confirmation of the Amino Acid Sequence of Ribonuclease T11The Journal of Biochemistry, 1985
- Refined structure of α-lytic protease at 1.7 Å resolution analysis of hydrogen bonding and solvent structureJournal of Molecular Biology, 1985
- Crystallographic Study of Mechanism of Ribonuclease Ti-Catalysed Specific RNA HydrolysisJournal of Biomolecular Structure and Dynamics, 1983
- Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray studyNature, 1982
- OCCURRENCE OF ASPARAGINE IN “DISALLOWED” CONFORMATIONS IN PROTEINSInternational Journal of Peptide and Protein Research, 1981
- Crystallization of a Complex between Ribonuclease T1 and 2'-Guanylic AcidEuropean Journal of Biochemistry, 1980
- Preferred backbone conformations of amino acid residues for solvent interactionJournal of Theoretical Biology, 1976