4o8u

Publication Abstract from PubMed

Sometimes crystals cannot diffract X-rays beyond 3.0 A 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 A 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.

Crystal structure of a novel non-Pfam protein PF2046 solved using low resolution B-factor sharpening and multi-crystal averaging methods.,Su J, Li Y, Shaw N, Zhou W, Zhang M, Xu H, Wang BC, Liu ZJ Protein Cell. 2010 May;1(5):453-8. doi: 10.1007/s13238-010-0045-7. Epub 2010 Jun , 4. PMID:21203960^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.