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Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.

Abstract:

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 polyethylene glycol 8000 as precipitant. The crystals (0.5-1.0 mm overall dimensions) diffract X-rays to at least 2.0 A resolution at synchrotrons and belong to space group P212121 with unit cell dimensio...

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Publication status:
Published

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Publisher copy:
10.1002/pro.5560040521

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Journal:
Protein science : a publication of the Protein Society More from this journal
Volume:
4
Issue:
5
Pages:
1007-1009
Publication date:
1995-05-01
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
Language:
English
Keywords:
Pubs id:
pubs:35653
UUID:
uuid:d4d9c434-089c-4b2e-aa2f-421b8ccf12cb
Local pid:
pubs:35653
Source identifiers:
35653
Deposit date:
2012-12-19

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