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.
Article
in English
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Conformation
/
Solubility
/
Bacterial Proteins
/
Models, Molecular
/
Chemistry
/
Crystallography, X-Ray
/
Pyrococcus furiosus
Type of study:
Prognostic study
Language:
English
Journal:
Protein & Cell
Year:
2010
Type:
Article
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