The National Synchrotron Light Source II (NSLS-II) has an opening for a 
post-doc to participate in multi-disciplinary research to help provide a 
molecular structural view of the mechanisms of nitrogenase-like enzymes. 
Collaborators at the Ohio State University have identified a previously 
uncharacterized enzymatic system that uses a nitrogenase-like reductase that is 
distinct from known nitrogenases and nitrogenase-like reductases. The work is 
supported by the DNA Synthesis Science program at the DOE Joint Genome 
Institute. Working in a multi-disciplinary, multi-national, team the candidate 
will carry out research using a macromolecular crystallography, solution 
scattering and cryogenic electron microscopy. This work will help establish a 
broader understanding of the molecular structures involved in electron delivery 
and catalytic reduction in this enzyme class.


Brookhaven National Laboratory is entering an exciting new chapter with one of 
the newest and most advanced synchrotron facilities in the world. National 
Synchrotron Light Source II (NSLS-II) enables the study of material properties 
and functions with nanoscale resolution and exquisite sensitivity by providing 
world-leading capabilities for X-ray imaging and high-resolution energy 
analysis.


This facility is open to users from academia and industry and its operations 
are at a time when the world enters a new era with a global economy fueled 
largely by scientific discoveries and technological innovations. NSLS-II 
provides the research tools needed to foster new discoveries and create 
breakthroughs in critical areas such as energy security, environment, and human 
health.

For further information regarding the position, and to begin the application 
process please visit the following link:

https://jobs.bnl.gov/job/upton/postdoctoral-research-associate-structural-biology/3437/4743704608

Thank you,
Dale



=============================
Dale Kreitler
National Synchrotron Light Source II
Building 745, Rm. 5L143
Upton, NY 11973
631-344-7318

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