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Three-Dimensional Structure of Cytochrome c Nitrite Reductase As Determined by Cryo-Electron Microscopy.


ABSTRACT: The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.

SUBMITTER: Baymukhametov TN 

PROVIDER: S-EPMC6209398 | biostudies-literature | 2018 Jul-Sep

REPOSITORIES: biostudies-literature

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Three-Dimensional Structure of Cytochrome c Nitrite Reductase As Determined by Cryo-Electron Microscopy.

Baymukhametov T N TN   Chesnokov Y M YM   Pichkur E B EB   Boyko K M KM   Tikhonova T V TV   Myasnikov A G AG   Vasiliev A L AL   Lipkin A V AV   Popov V O VO   Kovalchuk M V MV  

Acta naturae 20180701 3


The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme. ...[more]

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