1.6 A structure of semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with ribonuclease A from aqueous alcohol solutions.

Content Provider	Semantic Scholar
Author	Mel, S. J. De Doscher, Marilynn S. Martin, Philip D. Rodier, Francis Edwards, Brian F. P.
Copyright Year	1995
Abstract	The non-covalent combination of residues 1-118 of RNase A with a synthetic 14-residue peptide containing residues 111-124 of the molecule forms a highly active semisynthetic enzyme, RNase 1-118:111-124. With this enzyme, the roles played by the six C-terminal residues in generating the catalytic efficiency and substrate specificity of RNase can be studied using chemically synthesized analogs. The structure of RNase 1-118:111-124 from 43% aqueous ethanol has been determined using molecular-replacement methods and refined to a crystallographic R-factor of 0.166 for all observed reflections in the range 7.0-1.6 A (Protein Data Bank file ISSC). The structure is compared with the 2.0 A structure of RNase A from 43% aqueous 2-methyl-2-propanol and with the 1.8 A structure of the semisynthetic enzyme obtained from crystals grown in concentrated salt solution. The structure of RNase 1-118:111-124 from aqueous ethanol is virtually identical to that of RNase A from aqueous 2-methyl-2-propanol. Half of the crystallographically bound water molecules are not coincident, however. The structure is somewhat less similar to that of RNase 1-118:111-124 from salt solutions, with a major difference being the positioning of active-site residue His119.
File Format	PDF HTM / HTML
DOI	10.1107/S0907444995004574
PubMed reference number	15299768
Journal	Medline
Volume Number	51
Part	6
Alternate Webpage(s)	http://journals.iucr.org/d/issues/1995/06/00/se0172/se0172.pdf
Alternate Webpage(s)	https://doi.org/10.1107/S0907444995004574
Journal	Acta crystallographica. Section D, Biological crystallography
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article