A preliminary neutron crystallographic study of proteinase K at pD 6.5.
A preliminary neutron crystallographic study of the proteolytic enzyme proteinase K is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the vapor-diffusion method. Data were collected to a resolution of 2.3 A on the LADI-III diffractometer at the Institut Laue-Langevin (ILL) in 2.5 d. The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure with the aim of 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 the catalytic activity of proteinase K and to an enriched understanding of the subtilisin clan of serine proteases.
Gardberg
Anna S
AS
CSMB, Oak Ridge National Laboratory, USA. gardbergas@ornl.gov
Blakeley
Matthew P
MP
Myles
Dean A A
DA
D020134:Catalytic Domain; D018360:Crystallography, X-Ray / Q000379:methods; D019286:Endopeptidase K / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry; D033363:Neutron Diffraction / Q000379:methods*; D009502:Neutrons
D005656:Fungal Proteins; D019286:Endopeptidase K