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.
journal_name
Protein Celljournal_title
Protein & cellauthors
Su J,Li Y,Shaw N,Zhou W,Zhang M,Xu H,Wang BC,Liu ZJdoi
10.1007/s13238-010-0045-7subject
Has Abstractpub_date
2010-05-01 00:00:00pages
453-8issue
5eissn
1674-800Xissn
1674-8018journal_volume
1pub_type
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