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RESEARCH SCIENTIST/ ENGINEER 3

University of Washington

Job Description


As a UW employee, you have a unique opportunity to change lives on our campuses, in our state and around the world. UW employees offer their boundless energy, creative problem solving skills and dedication to build stronger minds and a healthier world.

UW faculty and staff also enjoy outstanding benefits, professional growth opportunities and unique resources in an environment noted for diversity, intellectual excitement, artistic pursuits and natural beauty. 

The Institute for Protein Design (IPD) at the University of Washington in Seattle is creating a new world of synthetic proteins to address 21st-century challenges in medicine, energy, and technology. The IPD is a unique interdisciplinary environment where world-class researchers with expertise in computing and software, biochemistry, genome sciences, biological structure, pharmacology, immunology and other basic science disciplines, as well as clinical medicine, work together to both computationally design and experimentally characterize novel biomolecules. Current projects include the design of novel therapeutics for cancer, neurological diseases, and more, as well as new vaccines, nanomaterials, and enzymes. For more detailed information about the Institute for Protein Design please see www.ipd.uw.edu .

The Department of Biochemistry has an outstanding opportunity for a Research Scientist/ Engineer 3.

The Research Scientist in Electron Microscopy will perform professional work in support of scientific research in biophysical characterization of computationally designed proteins and protein nanomaterials by EM methods. The research activities involve supporting protein EM structural characterization activities at the IPD. 

RESPONSIBILITIES:

• In this role, ~50% of effort will be dedicated to serving as an individual collaborator involved in specific protein design projects that required collaborative EM structural characterization.
• Another ~40% of the effort will be dedicated to assisting in the training and mentoring of other scientists in the use of EM instruments and EM methods for structural characterization of designed proteins.
• The remaining ~10% of effort will be dedicated to oversight of IPD EM instrumentation, interfacing with service personnel, and development of standard operating procedures for EM instrument use.

Representative Essential Duties and Responsibilities:
1.         Collaboration with numerous researchers at the IPD in EM characterization of de novo designed proteins and protein nanomaterials, including preparation of detailed reports on samples.
2.         Assists in training, and training others in how to train other research staff, postdoctoral fellows and graduate students at the IPD in EM characterization of de novo designed proteins and protein nanomaterials.
3.         Assists with complex multi-task projects for the EM characterization of de novo designed proteins and protein nanomaterials using several different electron microscopes.
4.  Processing and building of atomic/pseudo-atomic models derived data obtained by cryo-TEM (and potentially X-ray crystallography) methods.
5.         Participates in complex projects with uncertain outcomes requiring analysis from multiple perspectives.
6.         Oversight and partial responsibility for maintenance of IPD’s EM instruments, including coordinating analysis of a variety of samples from multiple researchers and labs in the IPD.
7.         Assists IPD Electron Microscopy Core Lead on projects with undefined time lines and uncertain outcomes requiring analysis from multiple perspectives.
8.         Uses expert knowledge and judgment to assist the IPD Electron Microscopy Research Core to implement new methods and techniques for obtaining solutions.

MINIMUM REQUIREMENTS:
Bachelor's Degree in Biochemistry, Structural Biology, Biophysics, and/or a related field + 3 years or more experience in related field.

Equivalent education/experience will substitute for all minimum qualifications except when there are legal requirements, such as a license/certification/registration.

ADDITIONAL REQUIREMENTS:
•          Ability to work and communicate regularly and professionally, as part of a team and independently, in written, visual, and oral formats is required.
•          Ability to mentor and train junior research staff on EM theory, standard operating procedures, software, and microscope operation.
•          Desire and ability to work as part of a large research team spanning over 100 people.
•   Technical proficiency, scientific creativity, collaborative ability as well as independent thought.
•          Expertise in protein structural characterization by either X-ray crystallography or single particle analysis (ns-TEM and/or cryo-TEM) methods, with an understanding of the underlying principles and concepts relating to protein structure determination by one or both methodologies is required.
•          Some prior experience with ns-TEM theory, sample preparation, microscope operation (i.e. ThermoFisher T12, TF20, Talos L120C or equivalent), data collection, and data processing (RELION, cisTEM and/or CryoSPARC) is highly preferred.
•          Some prior experience with cryo-TEM grid preparation is preferred.
•          Experience using COOT, Rosetta, PHENIX, and/or Chimera for EM-based protein structure determination and visualization is required.
•          Ability to work/navigate file systems via Linux terminal or equivalent.
•          Currently recognized as a resource for others to use in dealing with complex protein structure elucidation problems using either EM or X-ray crystallographic methods.
•          In-depth understanding of organizational structure both within and outside the work unit, including the role of each position in the group and in other groups.
•          Ability to help implement processes to achieve goals.  Will assist IPD Electron Microscopy •          Research Core Lead in directing others to develop essential tasks.
•          Helps review EM work activities of IPD research personnel to determine where new information could improve processes or move projects forward.
•          Ability to select and apply standardized scientific procedures and techniques to assignments of moderate complexity, involving potentially conflicting design requirements.

DESIRED:
An ideal candidate will be someone who (i) selects and applies standardized scientific procedures and techniques to assignments of moderate complexity, involving potentially conflicting design requirements, (ii) continually learns and helps implement new EM methods, (iii) can manage individual research projects that they own, (iv) can learn how to operate current and new EM instruments, (v) can learn to accurately process EM imaging data, or already has at least some prior experience doing so, (vi) has a deep desire to train others as a mentor in all of these areas, so that others within the IPD can successfully independently characterize protein structure by EM methods following efficient standard operating procedures, (vii) extensive prior experience with protein structure determination/model building using either EM and/or X-ray crystallography-derived data, (viii) and experience writing command-line scripts to help automate/semi-automate standard processes.

Application Process:

The application process for UW positions may include completion of a variety of online assessments to obtain additional information that will be used in the evaluation process.  These assessments may include Work Authorization, Cover Letter and/or others.  Any assessments that you need to complete will appear on your screen as soon as you select “Apply to this position”. Once you begin an assessment, it must be completed at that time; if you do not complete the assessment you will be prompted to do so the next time you access your “My Jobs” page. If you select to take it later, it will appear on your "My Jobs" page to take when you are ready. Please note that your application will not be reviewed, and you will not be considered for this position until all required assessments have been completed.


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