Your browser doesn't support javascript.
loading
Crystal structure of a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods
Protein & Cell ; (12): 453-458, 2010.
Artículo en Inglés | WPRIM | ID: wpr-757742
ABSTRACT
Sometimes crystals cannot diffract X-rays beyond 3.0 Å resolution due to the intrinsic flexibility associated with the protein. Low resolution diffraction data not only pose a challenge to structure determination, but also hamper interpretation of mechanistic details. Crystals of a 25.6 kDa non-Pfam, hypothetical protein, PF2046, diffracted X-rays to 3.38 Å resolution. A combination of Se-Met derived heavy atom positions with multiple cycles of B-factor sharpening, multi-crystal averaging, restrained refinement followed by manual inspection of electron density and model building resulted in a final model with a R value of 23.5 (R(free)= 24.7). The asymmetric unit was large and consisted of six molecules arranged as a homodimer of trimers. Analysis of the structure revealed the presence of a RNA binding domain suggesting a role for PF2046 in the processing of nucleic acids.
Asunto(s)
Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Conformación Proteica / Solubilidad / Proteínas Bacterianas / Modelos Moleculares / Química / Cristalografía por Rayos X / Pyrococcus furiosus Tipo de estudio: Estudio pronóstico Idioma: Inglés Revista: Protein & Cell Año: 2010 Tipo del documento: Artículo

Similares

MEDLINE

...
LILACS

LIS

Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Conformación Proteica / Solubilidad / Proteínas Bacterianas / Modelos Moleculares / Química / Cristalografía por Rayos X / Pyrococcus furiosus Tipo de estudio: Estudio pronóstico Idioma: Inglés Revista: Protein & Cell Año: 2010 Tipo del documento: Artículo