Purification, crystallization and preliminary X-ray analysis of Caenorhabditis elegans ubiquitin-conjugation enzyme M7.1.
Acta Crystallogr D Biol Crystallogr
; 59(Pt 3): 544-6, 2003 Mar.
Article
em En
| MEDLINE
| ID: mdl-12595721
ABSTRACT
M7.1 is a class IV ubiquitin-conjugation enzyme (UBC) that belongs to the ubiquitination cascade in Caenorhabditis elegans. The clone for this UBC has been overexpressed in Escherichia coli and the 16.7 kDa protein was purified from the soluble fraction. M7.1 was crystallized by sitting-drop vapor diffusion in 10% ethanol, 1.5 M NaCl at 277.5 K. Crystals diffracted to 1.75 A and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 44.3, b = 54.3, c = 60.2 A. The asymmetric unit contains a single monomer. A molecular-replacement model has been determined and refinement is in progress.
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Base de dados:
MEDLINE
Assunto principal:
Caenorhabditis elegans
/
Proteínas de Caenorhabditis elegans
/
Enzimas de Conjugação de Ubiquitina
/
Ligases
Limite:
Animals
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article