5 research outputs found

    Residues at the hydrophobic interface between AscE and AscG<sub>1–61</sub>.

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    <p>Ribbon representation of the AscE-AscG<sub>1–61</sub> crystal structure showing side chains of residues involved in the hydrophobic interface between AscE (blue) and AscG<sub>1–61</sub> (red), at two different views.</p

    Thermal denaturation of AscE-AscG, AscE-AscG<sub>1–61</sub>, AscE-AscG-AscF and AscE-AscG-AscF<sub>53–87</sub> complexes monitored by Far-UV CD.

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    <p>Thermal denaturation of the AscE-AscG<sub>1–61</sub> (closed circle), AscE-AscG full length (open circle), AscE-AscG-AscF<sub>53–87</sub> (closed square) and AscE-AscG-AscF full length (open square) complexes monitored by Far-UV CD at 220 nm from 10°C to 85°C.</p

    Superposition of the structure AscE-AscG<sub>1–61</sub> with PscE-PscF-PscG and YscE-YscF-YscG.

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    <p>The crystal structure of AscE-AscG<sub>1–61</sub> was superpositioned with (A) PscE-PscF-PscG or (B) YscE-YscF-YscG at two different views. The AscE and AscG<sub>1–61</sub> proteins are colored blue and red, respectively. The E, F and G proteins in the PscE-PscF-PscG or YscE-YscF-YscG complexes are colored magenta, green and cyan, respectively.</p

    Surface diagram of the AscE-AscG<sub>1–61</sub> complex and predicted AscF interacting residues.

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    <p>Surface diagram of the AscE-AscG<sub>1–61</sub> complex showing the tight interaction between AscE (blue) and AscG<sub>1–61</sub> (white), at two different views. The residues on AscG<sub>1–61</sub> predicted to interact with AscF based on the crystal structures of PscE-PscF-PscG and YscE-YscF-YscG are colored red. The surface diagrams were generated using the software Chimera <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0019208#pone.0019208-Pettersen1" target="_blank">[44]</a>.</p

    Crystallographic data and Refinement Statistics.

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    a<p>R<sub>sym</sub> = |I<sub>i</sub>−<i>|/|I<sub>i</sub>| where I<sub>i</sub> is the intensity of the i<sup>th</sup> measurement, and <i> is the mean intensity for that reflection.</i></i></p><i><i>b<p>R<sub>work</sub> = |F<sub>obs</sub>−F<sub>calc</sub>|/|F<sub>obs</sub>| where F<sub>calc</sub> and F<sub>obs</sub> are the calculated and observed structure factor amplitudes respectively.</p>c<p>R<sub>free</sub> = as for R<sub>work</sub>, but for 10.0% of the total reflections chosen at random and omitted from refinement.</p></i></i
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