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PDBsum entry 6cla
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PDB id:
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Hydrolase
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Title:
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2.80 a microed structure of proteinase k at 6.0 e- / a^2
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Structure:
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Proteinase k. Chain: a. Fragment: unp residues 106-384. Synonym: endopeptidase k, tritirachium alkaline proteinase. Ec: 3.4.21.64
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Source:
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Parengyodontium album. Engyodontium album, tritirachium album. Organism_taxid: 37998
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Authors:
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J.Hattne,D.Shi,C.Glynn,C.-T.Zee,M.Gallagher-Jones,M.W.Martynowycz, J.A.Rodriguez,T.Gonen
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Key ref:
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J.Hattne
et al.
(2018).
Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.
Structure,
26,
759.
PubMed id:
DOI:
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Date:
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02-Mar-18
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Release date:
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16-May-18
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PROCHECK
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Headers
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References
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P06873
(PRTK_PARAQ) -
Proteinase K from Parengyodontium album
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Seq:
Struc:
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384 a.a.
279 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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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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DOI no:
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Structure
26:759
(2018)
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PubMed id:
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Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.
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J.Hattne,
D.Shi,
C.Glynn,
C.T.Zee,
M.Gallagher-Jones,
M.W.Martynowycz,
J.A.Rodriguez,
T.Gonen.
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ABSTRACT
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Micro-crystal electron diffraction (MicroED) combines the efficiency of electron
scattering with diffraction to allow structure determination from nano-sized
crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to
solve structures of a diverse set of biomolecules and materials, in some cases
to sub-atomic resolution. However, little is known about the damaging effects of
the electron beam on samples during such measurements. We assess global and
site-specific damage from electron radiation on nanocrystals of proteinase K and
of a prion hepta-peptide and find that the dynamics of electron-induced damage
follow well-established trends observed in X-ray crystallography. Metal ions are
perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated
while the diffracted intensities decay exponentially with increasing exposure.
A better understanding of radiation damage in MicroED improves our assessment
and processing of all types of cryo-EM data.
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Links
