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Literature summary for 3.4.21.1 extracted from

  • Lazar, L.M.; Fisher, S.Z.; Moulin, A.G.; Kovalevsky, A.; Novak, W.R.; Langan, P.; Petsko, G.A.; Ringe, D.
    Time-of-flight neutron diffraction study of bovine gamma-chymotrypsin at the Protein Crystallography Station (2011), Acta Crystallogr. Sect. F, 67, 587-590.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
time-of-flight neutron diffraction data collected from gamma-chymotrypsin to 2.0 A resolution. The catalytic histidine is doubly deuterated. The serine and aspartate that make up the remainder of the catalytic triad do not show density corresponding to the presence of deuterium. There is also deuteration of backbone NH at terminal positions of beta-sheets Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00766
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