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Crystals 2018, 8(12), 460; https://doi.org/10.3390/cryst8120460

Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P65

1
Institute for Photonics and Advanced Sensing (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide 5005, Australia
2
School of Agriculture, Food and Wine, Department of Plant Science, The University of Adelaide, Adelaide 5005, Australia
3
Institute for Photonics and Advanced Sensing (IPAS), Department of Chemistry, and the Centre for Nanoscale BioPhotonics, The University of Adelaide, Adelaide 5005, Australia
*
Author to whom correspondence should be addressed.
Received: 21 November 2018 / Revised: 4 December 2018 / Accepted: 7 December 2018 / Published: 10 December 2018
(This article belongs to the Section Biomolecular Crystals)
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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. View Full-Text
Keywords: trypsin-like serine protease; endopeptidase; hydrolase trypsin-like serine protease; endopeptidase; hydrolase
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Marshall, A.C.; Keiller, B.G.; Pederick, J.L.; Abell, A.D.; Bruning, J.B. Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P65. Crystals 2018, 8, 460.

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