Literature DB >> 11679757

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

C E Nichols1, S Cocklin, A Dodds, J Ren, H Lamb, A R Hawkins, D K Stammers.   

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 A. Crystal form B belongs to space group C2, with unit-cell parameters a = 148.8, b = 64.3, c = 110.2 A, beta = 121.8 degrees.

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Year:  2001        PMID: 11679757     DOI: 10.1107/s090744490101410x

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases.

Authors:  D K Stammers; J Ren; K Leslie; C E Nichols; H K Lamb; S Cocklin; A Dodds; A R Hawkins
Journal:  EMBO J       Date:  2001-12-03       Impact factor: 11.598

2.  Modulation of the ligand binding properties of the transcription repressor NmrA by GATA-containing DNA and site-directed mutagenesis.

Authors:  Heather K Lamb; Jingshan Ren; Alison Park; Christopher Johnson; Kris Leslie; Simon Cocklin; Paul Thompson; Christopher Mee; Alan Cooper; David K Stammers; Alastair R Hawkins
Journal:  Protein Sci       Date:  2004-11-10       Impact factor: 6.725

  2 in total

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