Crystal structure of the specificity domain of ribonuclease P
- Author
- KRASILNIKOV, Andrey S1 ; XIAOJING YANG1 ; TAO PAN2 ; MONDRAGON, Alfonso1
[1] Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, United States
[2] Department of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, United States - Source
Nature (London). 2003, Vol 421, Num 6924, pp 760-764, 5 p ; ref : 30 ref
- CODEN
- NATUAS
- ISSN
- 0028-0836
- Scientific domain
- Multidisciplinary
- Publisher
- Nature Publishing, London
- Publication country
- United Kingdom
- Document type
- Article
- Language
- English
- Keyword (fr)
- Bacillus subtilis Conformation Domaine moléculaire Interaction moléculaire Ribonuclease P Site Spécificité Structure cristalline Bacillaceae Bacillales Bactérie Enzyme Esterases Hydrolases
- Keyword (en)
- Bacillus subtilis Conformation Molecular domain Molecular interaction Ribonuclease P Site Specificity Crystalline structure Bacillaceae Bacillales Bacteria Enzyme Esterases Hydrolases
- Keyword (es)
- Bacillus subtilis Conformación Dominio molecular Interacción molecular Ribonuclease P Sitio Especificidad Estructura cristalina Bacillaceae Bacillales Bacteria Enzima Esterases Hydrolases
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02C Nucleic acids / 002A02C04 Rna, ribonucleoproteins
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03G Structure in molecular biology / 002A03G03 Crystalline structure
- Discipline
- Analytical, structural and metabolic biochemistry Molecular biophysics
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 14523940
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1038/nature01386 
https://dx.doi.org/10.1038/nature01386
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