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Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P65
- Source :
- Crystals, Vol 8, Iss 12, p 460 (2018)
- Publication Year :
- 2018
- Publisher :
- MDPI AG, 2018.
-
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.
- Subjects :
- trypsin-like serine protease
endopeptidase
hydrolase
Crystallography
QD901-999
Subjects
Details
- Language :
- English
- ISSN :
- 20734352
- Volume :
- 8
- Issue :
- 12
- Database :
- Directory of Open Access Journals
- Journal :
- Crystals
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.895e35ea6c4e7684bf717ce778b6fa
- Document Type :
- article
- Full Text :
- https://doi.org/10.3390/cryst8120460