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<p class="MsoBodyText"><b class=""><span class="" style="font-size: 11pt; font-family: Arial;">Cryo-EM postdoc position in the Hinshaw Lab at NIH<o:p class=""></o:p></span></b></p>
<p class="MsoBodyText"><span class="" style="font-size: 11pt; font-family: Arial;">We are seeking a highly motivated candidate for the position of a postdoctoral fellow interested in structure-function studies of dynamin proteins. We are investigating the dynamic
properties of dynamin proteins by <b class="">cryo-EM</b>, biochemical and fluorescent microscopy approaches. Dynamin family members are large GTPases involved in numerous membrane fission and fusion events in the cell. Dynamin is crucial for endocytosis,
synaptic membrane recycling, and membrane trafficking within the cell. Mutations in dynamin have been shown to cause the peripheral neuropathy, Charcot-Marie-Tooth disease (CMT), centronuclear myopathy (CNM) and Hereditary Spastic Paraplegia (HSP). Other
dynamin family members are involved in processes including division and fusion of mitochondria (Drp1, Mfn, Opa1), and anti-viral activity (Mx, hGBP1). Mutations in Opa1 (Optic Atrophy) are a leading cause of blindness while mutations in Mfns (mitofusins)
lead to CMT and hereditary motor and sensory neuropathy (HMSM). We are currently exploring the structure and function of dynamin, mitofusins and Opa1 and how specific mutations lead to a disease state. <o:p class=""></o:p></span></p>
<p class="MsoBodyText"><span class="" style="font-family: Arial; font-size: 11pt;">The laboratory has excellent resources for cryo-electron microscopy and fluorescent microscopy. Our group has an FEI T12 and TF20 with a </span><b class="" style="font-family: Arial; font-size: 11pt;">K2
Summit</b><span class="" style="font-family: Arial; font-size: 11pt;"> direct electron detector. In addition, our institute (NIDDK) will have a 25% resource share on a FEI Titan </span><b class="" style="font-family: Arial; font-size: 11pt;">Krios</b><span class="" style="font-family: Arial; font-size: 11pt;"> with
an energy filter and K2 Summit camera, which will be installed on the NIH campus in the near future.</span></p>
<p class="MsoBodyText"><span class="" style="font-family: Arial; font-size: 11pt;">With its diverse laboratories and expertise available on the Bethesda main campus, and excellent research and clinical seminars, NIH provides a superb and stimulating scientific
environment that greatly enhances the postdoctoral training experience.</span></p>
<p class="MsoNormal"><span class="" style="font-family: Arial; font-size: 11pt;">The ideal candidate will have expertise in protein biochemistry (protein expression and purification) and/or cryo-EM methods including image processing.</span><span class="" style="font-family: Arial; font-size: 11pt;"> </span></p>
<p class="MsoNormal"><span class="" style="font-size: 11pt; font-family: Arial;">Applicants should send a cover letter, briefly describing previous research experience and future goals, a CV and </span><span class="" style="font-size: 11pt; font-family: Arial;">contact
information for three professional references to <a href="mailto:jennyh@niddk.nih.gov" class="">jennyh@niddk.nih.gov</a> .</span></p>
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<div class="">Jenny Hinshaw</div>
<div class="">Section Chief, Structural Cell Biology</div>
<div class="">LCMB, NIDDK</div>
<div class="">National Institute of Health</div>
<div class="">8 Center Dr, Bld 8, Rm 1A03</div>
<div class="">Bethesda, MD 20892 USA</div>
<div class=""><a href="mailto:jennyh@niddk.nih.gov" class="">jennyh@niddk.nih.gov</a></div>
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