Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
Recombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyeth...
Prif Awduron: | Roach, P, Schofield, C, Baldwin, J, Clifton, I, Hajdu, J |
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Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
1995
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Eitemau Tebyg
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Glutamine-330 is not essential for activity in isopenicillin N synthase from Aspergillus nidulans.
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Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.
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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes.
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Anaerobic crystallisation of an isopenicillin N synthase.Fe(II).substrate complex demonstrated by X-ray studies.
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