Postdoctoral Research Fellow - Xray Crystallography
Who We Are
At the Roche Group, about 80,000 people across 150 countries are pushing back the frontiers of healthcare. Working together, we've become one of the world's leading research-focused healthcare groups. A member of the Roche Group, Genentech has been at the forefront of the biotechnology industry for more than 30 years, using human genetic information to develop novel medicines for serious and life-threatening diseases. The headquarters for Roche pharmaceutical operations in the United States, Genentech has multiple therapies on the market for cancer and other serious illnesses. Please take this opportunity to learn about Genentech, where we believe that our employees are our most important asset and are dedicated to remaining a great place to work.
The Position
Crystallography Post Doctoral Fellow - Hymowitz Lab
Responsibilities:
A position is available for a postdoctoral fellow with expertise in crystallography to join the Department of Structural Biology at Genentech, Inc. Active areas of research include the structure and function of intracellular signaling cascades involving ubiquitin as well as the structure and function of protein complexes relevant to human disease. The successful candidate will be involved in all aspects of crystallography, including expression and purification of proteins, crystallization, data collection, structure determination and analysis of protein structures.
Who You Are
Highly motivated candidates are sought who are capable of independent work in a collaborative environment. Candidates must have a Ph.D. in structural biology, biophysics, biochemistry or related discipline. Candidates should have a strong background in protein crystallography and structure determination as well as demonstrated by successful purification, characterization and crystallization of challenging proteins as evidenced by a first author paper published or accepted in a peer-reviewed journal. Familiarity with biophysical techniques is a plus.
The crystal structure of the catalytic domain of the NF-¿B inducing kinase reveals a narrow but flexible active site.
de Leon-Boenig G, Bowman KK, Feng JA, Crawford T, Everett C, Franke Y, Oh A, Stanley M, Staben ST, Starovasnik MA, Wallweber HJ, Wu J, Wu LC, Johnson AR, Hymowitz SG.
Structure. 2012 Oct 10;20(10):1704-14. doi: 10.1016/j.str.2012.07.013. Epub 2012 Aug 23.
PMID: 22921830 [PubMed - in process]
Related citations
Ubiquitin binding to A20 ZnF4 is required for modulation of NF-¿B signaling.
Bosanac I, Wertz IE, Pan B, Yu C, Kusam S, Lam C, Phu L, Phung Q, Maurer B, Arnott D, Kirkpatrick DS, Dixit VM,Hymowitz SG.
Mol Cell. 2010 Nov 24;40(4):548-57. doi: 10.1016/j.molcel.2010.10.009.
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Genentech is an Equal Opportunity Employer.
