Work

Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P65

Year: 2018

Type: article

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 α-chymotrypsin was crystallized at neutral pH using ammonium sulphate as the precipitant, resulting in crystals that conform to P65 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 α-chymotrypsin grown at low pH in space group P21.

Source: Crystals

DOI: 10.3390/cryst8120460

Authors: Andrew Marshall, Benjamin Keiller, Jordan Pederick, Andrew Abell, John Bruning

Institution: The University of Adelaide

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: gold

Estimated APC paid: $2,534

Funders: Australian Nuclear Science and Technology Organisation, Australian Synchrotron, Australian Research Council