http://www.cnr.it/ontology/cnr/individuo/prodotto/ID227763
The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue; hydration and stereochemical analysis (Articolo in rivista)
- Type
- Label
- The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue; hydration and stereochemical analysis (Articolo in rivista) (literal)
- Anno
- 2000-01-01T00:00:00+01:00 (literal)
- Alternative label
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L. (2000)
The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue; hydration and stereochemical analysis
in Journal of Molecular Biology
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L. (literal)
- Pagina inizio
- Pagina fine
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- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 4, I-80134, Napoli, Italy
Dipartimento di Chimica Università di Napoli \"Federico II'', Via Mezzocannone 4, I-80134, Napoli, Italy (literal)
- Titolo
- The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue; hydration and stereochemical analysis (literal)
- Abstract
- Crystals of the deamidated form of bovine pancreatic ribonuclease which
contains an isoaspartyl residue in position 67 diffract to 0.87 Ang. at 100 K.
We have refined the crystallographic model using anisotropic displacement
parameters for all atoms to a conventional crystallographic residual
R 0.101 for all observed reflections in the resolution range 61.0-0.87 Ang.
The ratio observations/parameters is 7.2 for the final model. This structure
represents one of the highest resolution protein structures to date
and interestingly, it is the only example containing more than one molecule
in the asymmetric unit with a resolution better than 1.0 Ang. The
non-crystallographic symmetry has been used as a validation check of
the geometrical parameters and it has allowed an estimate for an upper
limit of errors associated with this high resolution model. In the present
structure it was possible to obtain a more accurate picture of the active
site whose electron density was not clearly interpretable in the previous
1.9 Ang. resolution structure. In particular, the P1 site is alternatively occupied
either by a sulphate anion or by a water molecule network. Most of
hydrogen atoms were visible in the electron density maps, including
those involved in Ca-Ha...?O interactions. Analysis of protein-solvent
interactions has revealed the occurrence of an extensive cluster of water
molecules, predominantly arranged in pentagonal fused rings and surrounding
hydrophobic moiety of side-chains. Finally, in spite of the limited
sample of residues, we have detected a clear dependence of
backbone N-Ca-C angle on residue conformation. This correlation can
be fruitfully used as a valuable tool in protein structure validation. (literal)
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