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

Citation
Ce. Nichols et al., Expression, purification and crystallization of Aspergillus nidulans NmrA,a negative regulatory protein involved in nitrogen-metabolite repression, ACT CRYST D, 57, 2001, pp. 1722-1725
Citations number
14
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
11
Pages
1722 - 1725
Database
ISI
SICI code
0907-4449(200111)57:<1722:EPACOA>2.0.ZU;2-#
Abstract
The NmrA repressor protein of Aspergillus nidulans was overproduced in Esch erichia coli and purified to homogeneity. Gel-exclusion chromatography show ed that NmrA was monomeric in solution under the buffer conditions used. Th e protein was crystallized in three forms, belonging to trigonal, monoclini c and hexagonal space groups. Two of these crystal forms (A and B) diffract to high resolution and thus appear suitable for structure determination. C rystal 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 = 1 21.8 degrees.