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...
المؤلفون الرئيسيون: | Fujishima, Y, Nordlund, P, Pelosi, G, Schofield, C, Cole, S, Baldwin, J, Hajdu, J |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1994
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مواد مشابهة
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Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
حسب: Roach, P, وآخرون
منشور في: (1995) -
Isolation and partial characterisation of ACV synthetase from Cephalosporium acremonium and Streptomyces clavuligerus.
حسب: Baldwin, J, وآخرون
منشور في: (1990) -
EXAFS STUDIES OF ISOPENICILLIN-N SYNTHASE
حسب: Randall, C, وآخرون
منشور في: (1992) -
Molecular weight analysis of isopenicillin N synthase by electrospray mass spectrometry.
حسب: Aplin, RT, وآخرون
منشور في: (1990) -
ISOPENICILLIN-N SYNTHASE - A NEW MODE OF REACTIVITY
حسب: Baldwin, J, وآخرون
منشور في: (1991)