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Expression, purification and crystallization of Aspergillus nidulans NmrA, a negative regulatory protein involved in nitrogen-metabolite repression

Lookup NU author(s): Dr Simon Cocklin, Dr Anna Dodds, Dr Heather Lamb, Professor Alastair Hawkins

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Abstract

The NmrA repressor protein of Aspergillus nidulans was overproduced in Escherichia coli and purified to homogeneity. Gel-exclusion chromatography showed that NmrA was monomeric in solution under the buffer conditions used. The protein was crystallized in three forms, belonging to trigonal, monoclinic and hexagonal space groups. Two of these crystal forms (A and B) diffract to high resolution and thus appear suitable for structure determination. Crystal form A belongs to space group P3((1))21, with unit-cell parameters a = b = 76.8, c = 104.9 Angstrom. Crystal form B belongs to space group C2, with unit-cell parameters a = 148.8, b = 64.3, c = 110.2 Angstrom, beta = 121.8 degrees.

Publication metadata

Author(s): Hawkins AR; Lamb H; Dodds A; Cocklin S; Nichols CE; Ren J; Stammers DK

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica Section D: Biological Crystallography

Year: 2001

Volume: 57

Issue: 11

Pages: 1722-1725

ISSN (print): 0907-4449

ISSN (electronic): 1399-0047

Publisher: Wiley-Blackwell Publishing, Inc.

URL: http://dx.doi.org/10.1107/S090744490101410X

DOI: 10.1107/S090744490101410X

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