Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein
AUTOR(ES)
Ambrazi, Maria
FONTE
International Union of Crystallography
RESUMO
The double mutant D30P/A31G of the Rop protein was crystallized with the aim of analyzing the loop region as a possible folding-control element. The crystals belonged to space group P21 and diffracted to 1.4 Å resolution.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2376389Documentos Relacionados
- Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin
- Purification, crystallization and preliminary X-ray diffraction analysis of a plant subtilase
- Purification, crystallization and preliminary X-ray diffraction analysis of an oomycete-derived Nep1-like protein
- Purification, crystallization and preliminary X-ray diffraction analysis of human Gadd45γ
- Purification, crystallization and preliminary X-ray diffraction analysis of disease-related mutants of p97