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...
Автори: | Fujishima, Y, Nordlund, P, Pelosi, G, Schofield, C, Cole, S, Baldwin, J, Hajdu, J |
---|---|
Формат: | Journal article |
Мова: | English |
Опубліковано: |
1994
|
Схожі ресурси
-
Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
за авторством: Roach, P, та інші
Опубліковано: (1995) -
Isolation and partial characterisation of ACV synthetase from Cephalosporium acremonium and Streptomyces clavuligerus.
за авторством: Baldwin, J, та інші
Опубліковано: (1990) -
EXAFS STUDIES OF ISOPENICILLIN-N SYNTHASE
за авторством: Randall, C, та інші
Опубліковано: (1992) -
Molecular weight analysis of isopenicillin N synthase by electrospray mass spectrometry.
за авторством: Aplin, RT, та інші
Опубліковано: (1990) -
ISOPENICILLIN-N SYNTHASE - A NEW MODE OF REACTIVITY
за авторством: Baldwin, J, та інші
Опубліковано: (1991)