Literature summary for 4.6.1.18 extracted from

Yagi, D.; Yamada, T.; Kurihara, K.; Ohnishi, Y.; Yamashita, M.; Tamada, T.; Tanaka, I.; Kuroki, R.; Niimura, N.
A neutron crystallographic analysis of phosphate-free ribonuclease A at 1.7 A resolution (2009), Acta Crystallogr. Sect. D, 65, 892-899.

Crystallization (Commentary)

Crystallization (Comment)	Organism
neutron crystallographic analysis of phosphate-free bovine pancreatic RNase A, 50% tert-butyl alcohol, temperature 298 K, then the crystal is soaked in heavy water solution, pH 6.2, for two months, BATCH, space group P1211, resolution 1.7 A, His12 acts mainly as a general base in the catalytic process of Rnase A, numerous other distinctive structural features such as the hydrogen positions of methyl groups, hydroxyl groups, prolines, asparagines and glutamines are also determined	Bos taurus

Crystallization (Comment)

Organism

neutron crystallographic analysis of phosphate-free bovine pancreatic RNase A, 50% tert-butyl alcohol, temperature 298 K, then the crystal is soaked in heavy water solution, pH 6.2, for two months, BATCH, space group P1211, resolution 1.7 A, His12 acts mainly as a general base in the catalytic process of Rnase A, numerous other distinctive structural features such as the hydrogen positions of methyl groups, hydroxyl groups, prolines, asparagines and glutamines are also determined

Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Bos taurus	-

Synonyms

Synonyms	Comment	Organism
pancreatic ribonuclease A	-	Bos taurus
RNase A	-	Bos taurus

General Information

General Information	Comment	Organism
physiological function	His12 acts mainly as a general base in the catalytic process of RNase A	Bos taurus

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Release 2023.1 (January 2023)