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Crystallization and preliminary X-ray diffraction analysis of full-length and proteolytically activated pyruvate oxidase from Escherichia coli

The thiamine diphosphate- and flavin-dependent peripheral membrane enzyme pyruvate oxidase from Escherichia coli (EcPOX) has been crystallized in the full-length form and as a proteolytically activated C-terminal truncation variant which lacks the last 23 amino acids (Δ23 EcPOX). Crystals were grown...

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Hlavní autoři: Weidner, Annett, Neumann, Piotr, Wille, Georg, Stubbs, Milton T., Tittmann, Kai
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2008
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2374146/
https://ncbi.nlm.nih.gov/pubmed/18323602
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309108003473
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