Fadel A. Samatey Group (Japanese): Difference between revisions

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'''<span style="font-size:200%">サマテイ研</span>'''
'''<span style="font-size:200%">サマテイ研</span>'''[[en:Fadel A. Samatey Group]]


<font color="red">Translation of this article to Japanese is in progress.</font>
<font color="red">Translation of this article to Japanese is in progress.</font>


<table align="right" width="260" ><tr><td rowspan="2">&nbsp;</td><td>[[Image:Flagellar hook em density 1ucu.jpg]]</td></tr><tr><td><font color="#00908c">Crystal structure of flagellar hook</font> fitted into <font color="magenta">electron density map</font> obtained by electron cryomicroscopy<ref name="hook1">PMID:15510139</ref>.</td></tr></table>
<table align="right" width="260" ><tr><td rowspan="2">&nbsp;</td><td>[[Image:Flagellar hook em density 1ucu.jpg]]</td></tr><tr><td><font color="#00908c">Crystal structure of flagellar hook</font> fitted into <font color="magenta">electron density map</font> obtained by electron cryomicroscopy<ref name="hook1">PMID:15510139</ref>.</td></tr></table>
:[[Fadel A. Samatey Group|This page in English]]
 
[[User:Fadel A. Samatey|Fadel A. Samatey]] is Head of the [http://www.oist.jp/en/research/research-units/unit-transmem-traffick.html Transmembrane Trafficking Unit] at the [http://oist.jp Okinawa Institute of Science and Technology (OIST)]. Samatey's group uses [[X-ray crystallography]], genetic and biochemical approaches to elucidate the structures and functions of transmembrane proteins, especially type III secretion proteins in [[Flagella, bacterial|bacterial flagella]].
[[User:Fadel A. Samatey|Fadel A. Samatey]] is Head of the [http://www.oist.jp/en/research/research-units/unit-transmem-traffick.html Transmembrane Trafficking Unit] at the [http://oist.jp Okinawa Institute of Science and Technology (OIST)] (Japan). Samatey's group uses [[X-ray crystallography]], genetic and biochemical approaches to elucidate the structures and functions of transmembrane proteins, especially type III secretion proteins in [[Flagella, bacterial|bacterial flagella]].


[[#Contributions from OIST|Below]] are listed contributions from the Samatey Group, most recent first.
[[#Contributions from OIST|Below]] are listed contributions from the Samatey Group, most recent first.
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<ref group="xtra">PMID: 15510139</ref><references group="xtra" />
<ref group="xtra">PMID: 15510139</ref><references group="xtra" />


:<table style="background: #ffd0b0;padding: 6px;"><tr><td>Reports the first structure of the major fragment of the protein monomer that assembles into the '''[[Flagellar hook of bacteria|bacterial flagellar hook]]''' ([[1wlg]], 1.8 &Aring; [[resolution]]). Fits the monomer into an electron cryomicroscopic density map, resulting in straight and curved models of the hook, including a rotating model.</td></tr></table>
:<table style="background: #ffd0b0;padding: 6px;"><tr><td>Reports the first structure of a major fragment of the protein monomer that assembles into the '''[[Flagellar hook of bacteria|bacterial flagellar hook]]''' ([[1wlg]], 1.8 &Aring; [[resolution]]). Fits the monomer into an electron cryomicroscopic density map, resulting in straight and curved models of the hook, including a rotating model.</td></tr></table>




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<ref group="xtra">PMID: 11268201</ref><references group="xtra" />
<ref group="xtra">PMID: 11268201</ref><references group="xtra" />


:<table style="background: #ffd0b0;padding: 6px;"><tr><td>Reports, for the first time, the atomic structure of the major fragment of the protein chain monomer that assembles into the '''[[Flagellar filament of bacteria|bacterial flagellar filament]]''' ([[1io1]], 2.0 &Aring; [[resolution]]). The crystal contained chains of monomers, which revealed how the monomer protein chains fit together into protofilaments. Theoretical simulation revealed a possible mechanism for how the filament reverses direction, a mechanism crucial to how bacteria swim towards food or away from harm by reversing the flagellar motor.</td></tr></table>
:<table style="background: #ffd0b0;padding: 6px;"><tr><td>Reports, for the first time, the atomic structure of a major fragment of the protein chain monomer that assembles into the '''[[Flagellar filament of bacteria|bacterial flagellar filament]]''' ([[1io1]], 2.0 &Aring; [[resolution]]). The crystal contained chains of monomers, which revealed how the monomer protein chains fit together into protofilaments. Theoretical simulation revealed a possible mechanism for how the filament reverses direction, a mechanism crucial to how bacteria swim towards food or away from harm by reversing the flagellar motor.</td></tr></table>




<ref group="xtra">PMID: 11162732</ref><references group="xtra" />
<ref group="xtra">PMID: 11162732</ref><references group="xtra" />
<center><table width="450"><tr><td>[[Image:Protein crystals samatey.png]]</td><td>&nbsp;</td><td>Crystals of the [[Flagellar hook of bacteria|flagellar hook protein]] produced in the Samatey lab.</td></tr></table></center>


===1990's===
===1990's===
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==References==
==References==
<references />
<references />
[[en:Fadel A. Samatey Group]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Fadel A. Samatey, Eric Martz