$Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.$

Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.

Recombinant isopenicillin N synthase from Cephalosporium acremonium was expressed in Escherichia coli and the protein was purified. After nearly 5000 crystallization trials, the apo enzyme was crystallized by the hanging drop vapour diffusion technique, using polyethylene glycol and lithium sulphate...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Fujishima, Y, Nordlund, P, Pelosi, G, Schofield, C, Cole, S, Baldwin, J, Hajdu, J
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	1994

Παρόμοια τεκμήρια

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Glutamine-330 is not essential for activity in isopenicillin N synthase from Aspergillus nidulans.
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Anaerobic crystallisation of an isopenicillin N synthase center dot Fe(II)center dot substrate complex demonstrated by X-ray studies
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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes.
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Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase.
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Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate.
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X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis
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Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue.
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Occurrence of Isopenicillin-N-Synthase Homologs in Bioluminescent Ctenophores and Implications for Coelenterazine Biosynthesis.
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Production of functionally active <it>Penicillium chrysogenum </it>isopenicillin N synthase in the yeast <it>Hansenula polymorpha</it>
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Έκδοση: (2008-03-01)

The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.
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Spectroscopic studies reveal details of substrate-induced conformational changes distant from the active site in isopenicillin N synthase
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Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine.
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