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...

Szczegółowa specyfikacja

Opis bibliograficzny
Główni autorzy: Fujishima, Y, Nordlund, P, Pelosi, G, Schofield, C, Cole, S, Baldwin, J, Hajdu, J
Format: Journal article
Język:English
Wydane: 1994
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author Fujishima, Y
Nordlund, P
Pelosi, G
Schofield, C
Cole, S
Baldwin, J
Hajdu, J
author_facet Fujishima, Y
Nordlund, P
Pelosi, G
Schofield, C
Cole, S
Baldwin, J
Hajdu, J
author_sort Fujishima, Y
collection OXFORD
description 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 as precipitants. Two crystal forms have been obtained with either octahedral or elongated prismatic habits. The larger octahedral crystals (0.1 mm over-all dimensions) belong to space group I4 with unit cell dimensions of a = b = 124.7 A, c = 156.9 A, and diffract X-rays to about 3.5 A resolution at synchrotrons. The crystallographic asymmetric unit contains a dimer.
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spelling oxford-uuid:91f20160-2c46-4880-9390-cc5a0e26fad72022-03-26T23:22:03ZCrystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:91f20160-2c46-4880-9390-cc5a0e26fad7EnglishSymplectic Elements at Oxford1994Fujishima, YNordlund, PPelosi, GSchofield, CCole, SBaldwin, JHajdu, JRecombinant 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 as precipitants. Two crystal forms have been obtained with either octahedral or elongated prismatic habits. The larger octahedral crystals (0.1 mm over-all dimensions) belong to space group I4 with unit cell dimensions of a = b = 124.7 A, c = 156.9 A, and diffract X-rays to about 3.5 A resolution at synchrotrons. The crystallographic asymmetric unit contains a dimer.
spellingShingle Fujishima, Y
Nordlund, P
Pelosi, G
Schofield, C
Cole, S
Baldwin, J
Hajdu, J
Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title_full Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title_fullStr Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title_full_unstemmed Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title_short Crystallization and preliminary X-ray diffraction studies on a recombinant isopenicillin N synthase from Cephalosporium acremonium.
title_sort crystallization and preliminary x ray diffraction studies on a recombinant isopenicillin n synthase from cephalosporium acremonium
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