A preliminary neutron crystallographic study of proteinase K at pD 6.5
- ORNL
- Institut Laue-Langevin (ILL)
A preliminary neutron crystallographic study of the proteolytic enzyme proteinase K is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the vapour-diffusion method. Data were collected to a resolution of 2.3 Å on the LADI-III diffractometer at the Institut Laue Langevin (ILL) in 2.5 days. The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure aimed at providing relevant information on the location of H atoms, particularly at the active site. This information will contribute to further understanding of the molecular mechanisms underlying proteinase K's catalytic activity and to an enriched understanding of the subtilisin clan of serine proteases.
- Research Organization:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-00OR22725
- OSTI ID:
- 966096
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 2 Vol. 65; ISSN ACSFCL; ISSN 1744-3091
- Publisher:
- International Union of Crystallography
- Country of Publication:
- United States
- Language:
- English
Similar Records
Picornaviral 3C cysteine proteinases have a fold similar to the chymotrypsin-like serine proteinases