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...
Hlavní autoři: | Fujishima, Y, Nordlund, P, Pelosi, G, Schofield, C, Cole, S, Baldwin, J, Hajdu, J |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
1994
|
Podobné jednotky
-
Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
Autor: Roach, P, a další
Vydáno: (1995) -
Isolation and partial characterisation of ACV synthetase from Cephalosporium acremonium and Streptomyces clavuligerus.
Autor: Baldwin, J, a další
Vydáno: (1990) -
EXAFS STUDIES OF ISOPENICILLIN-N SYNTHASE
Autor: Randall, C, a další
Vydáno: (1992) -
Molecular weight analysis of isopenicillin N synthase by electrospray mass spectrometry.
Autor: Aplin, RT, a další
Vydáno: (1990) -
ISOPENICILLIN-N SYNTHASE - A NEW MODE OF REACTIVITY
Autor: Baldwin, J, a další
Vydáno: (1991)