Category: Science Highlights

Recent SAXS structures

SAXS capabilities of the SIBYLS beamline are demonstrated quite nicely in recent papers published in September and October. Datta AB, Hura GL, Wolberger C. “The structure and conformation of Lys63-linked tetraubiquitin.” J Mol Biol. 2009 Oct 9;392(5):1117-24. Epub 2009 Aug 4. Jain R, Hammel M, Johnson RE, Prakash L, Prakash S, Aggarwal AK. “Structural Insights…
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Nbs1 Flexibly Tethers Ctp1 and Mre11- Rad50 in DNA Double-Strand Break Repair

A paper has been published in The October 2 issue of Cell by Scott Williams *et al.* that sheds light on a previously missing piece of the double-strand break repair complex MRN (aka Mre11-Rad50-Nbs1). The paper entitled “Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and Repair” presents a compelling model…
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Structures of the Ribosome in Intermediate States of Ratcheting

Wen Zhang and Jack Dunkle in the Cate lab have a nice report out in the August 21, 2009 issue of Science describing their latest crystal structures of the E. coli ribosome with and without tRNA mimcs. These new structure shed light on the rachet-like action of the intact ribosome as it interacts with tRNA…
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Lysine Riboswitch on the Cover of September 2009 Issue of RNA

Cover Illustration from the September 2009 issue of RNA: Crystal structure of the lysine riboswitch bound to lysine (Protein Data Bank code: 3d0u) Image details show RNA: ribbon; lysine: space-filling representation, red; iridium hexamine ions: space-filling representation, blue. Abstract: Riboswitches are metabolite-sensitive elements found in mRNAs that control gene expression through a regulatory secondary structural…
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SAXS Clarifies Mechanism of DNA Recognition by Polynucleotide Kinase.

In this paper, published in Nucleic Acid Research, the authors used small-angle X-ray scattering (SAXS) combined with advanced computational approaches to characterize the conformational variability and DNA-binding properties of PNK. Extensive use of the SAXS capabilities of the SIBYLS beamline allowed the authors to visualize a flexible attachment of the FHA domain to the catalytic…
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Robust, High-Throughput Solution Structural Analysis by SAXS

In this paper, published online today in Nature Methods, the high-throughput SAXS capabilities of the SIBYLS beamline are demonstrated quite nicely. We present an efficient pipeline enabling high-throughput analysis of protein structure in solution with small angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling of microliter volumes, temperature and anaerobic control, rapid data…
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Structure and Flexibility Within Proteins as Identified Through SAXS

In a recent article in the General Physiology and Biophysics we describe an analysis tool using relatively inexpensive small angle X-ray scattering (SAXS) measurements to identify protein flexibility and validate a constructed minimal ensemble of models, which represent highly populated conformations in solution. The resolution of these results is sufficient to address the questions being…
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Flipping of Alkylated DNA Damage Bridges Base and Nucleotide Excision Repair

Julie Tubbs from John Tainer’s group at Scripps published a totally sweet paper in the June 11, 2009 issue of Nature demonstrating that the ATL protein uses nucleotide flipping to link alkylated base damage to the nucleotide excision repair pathway. This publication was in part made possible by the SIBYLS beamline.  Abstract: Alkyltransferase-like proteins (ATLs) share…
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