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PDBsum entry 5wrc
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Enzyme class:
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E.C.3.4.21.64
- peptidase K.
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Reaction:
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Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.
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Sci Rep
7:703
(2017)
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PubMed id:
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Hydroxyethyl cellulose matrix applied to serial crystallography.
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M.Sugahara,
T.Nakane,
T.Masuda,
M.Suzuki,
S.Inoue,
C.Song,
R.Tanaka,
T.Nakatsu,
E.Mizohata,
F.Yumoto,
K.Tono,
Y.Joti,
T.Kameshima,
T.Hatsui,
M.Yabashi,
O.Nureki,
K.Numata,
E.Nango,
S.Iwata.
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ABSTRACT
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Serial femtosecond crystallography (SFX) allows structures of proteins to be
determined at room temperature with minimal radiation damage. A highly viscous
matrix acts as a crystal carrier for serial sample loading at a low flow rate
that enables the determination of the structure, while requiring consumption of
less than 1 mg of the sample. However, a reliable and versatile carrier matrix
for a wide variety of protein samples is still elusive. Here we introduce a
hydroxyethyl cellulose-matrix carrier, to determine the structure of three
proteins. The de novo structure determination of proteinase K from
single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal
of the praseodymium atom was demonstrated using 3,000 diffraction images.
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Links
