Crystal structure of bovine alpha-chymotrypsin in space group P6(5)

Andrew C. Marshall, Benjamin G. Keiller, Jordan L. Pederick, Andrew D. Abell, John B. Bruning

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Chymotrypsin is a protease that is commonly used as a standard for protein crystallization and as a model system for studying serine proteases. Unliganded bovine alpha-chymotrypsin was crystallized at neutral pH using ammonium sulphate as the precipitant, resulting in crystals that conform to P6(5) symmetry with unit cell parameters that have not been reported previously. Inspection of crystallographic interfaces revealed that the major interface between any two molecules in the crystal lattice represents the interface of the biological dimer, as previously observed for crystals of unliganded alpha-chymotrypsin grown at low pH in space group P2(1).

Original languageEnglish
Article number460
Number of pages7
JournalCrystals
Volume8
Issue number12
DOIs
Publication statusPublished - Dec 2018
Externally publishedYes

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