@article {Gardberg:2009:1744-3091:184,
title = "A preliminary neutron crystallographic study of proteinase K at pD 6.5",
journal = "Acta Crystallographica Section F",
parent_itemid = "infobike://bpl/ayf2",
publishercode ="bp",
year = "2009",
volume = "65",
number = "2",
publication date ="2009-02-01T00:00:00",
pages = "184-187",
itemtype = "ARTICLE",
issn = "1744-3091",
url = "https://www.ingentaconnect.com/content/bpl/ayf2/2009/00000065/00000002/art00029",
doi = "doi:10.1107/S1744309109000566",
keyword = "proteinase K, serine protease, neutron diffraction",
author = "Gardberg, Anna S. and Blakeley, Matthew P. and Myles, Dean A. A.",
abstract = "A preliminary neutron crystallographic study of the proteolytic enzyme proteinase K is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the vapordiffusion method. Data were collected to a resolution of 2.3\AA on the
LADIIII diffractometer at the Institut LaueLangevin (ILL) in 2.5d. 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.",
}