• MX, Small Molecule Crystallography
• XAS, XFI

As an Industrial Support Scientist, Kurt Nienaber assists the Macromolecular Crystallography and Small Molecule Crystallography programs at the CLS for the Industry Services group. Utilizing his extensive education, synchrotron experiences, and successful collaboration with other scientists, Kurt is able to ensure the satisfaction of industrial partners.

A strong desire to continue learning has driven Kurt’s diverse higher education. Following the completion of his Biochemistry undergraduate degree, Kurt’s M.Sc. of Biochemistry at the University of Saskatchewan focused on utilizing Macromolecular Crystallography (MX) to correct a mischaracterization of an enzyme. While completing his Ph.D. in Geological Sciences at the University of Saskatchewan, Kurt used X-ray Absorption Spectroscopy (XAS) to study copper binding in the prion protein that causes Mad Cow Disease.  Kurt also utilized XAS to examine the role of common MX and XAS cryoprotectants and increased photoreduction.  Kurt’s continuing passion for Life Sciences and desire to aid individuals are a perfect fit for his role within the Industry Services team.

Outside of the CLS, Kurt can often be found at the golf course, curling rink, or spending quality time with his lovely family of five. In addition to his work at the CLS, Kurt continues to provide scientific advice to a local online school curriculum.

Nienaber, Kurt; Pushie, Jake; Cotelesage, Julien and Pickering, Ingrid. (2018). Cryoprotectants severely exacerbate x-ray induced photoreduction. Journal of Physical Chemistry 9(3), 540-544. 10.1021/acs.jpclett.7b03111

---

Nienaber, Kurt; Nehzati, Susan; Cotelesage, Julien; Pickering, Ingrid and George, Graham. (2018). X-ray-induced photoreduction of Hg(II) in aqueous frozen solution yields nearly monatomic Hg(0). Inorganic Chemistry 57(14), 8205-8210. 10.1021/acs.inorgchem.8b00694

---

Pushie, Jake; Nienaber, Kurt; McDonald, Alex; Millhauser, Glenn and George, Graham. (2014). Combined EXAFS and DFT structure calculations provide structural insights into the 1:1 multi-histidine complexes of Cu(II), Cu(I), and Zn(II) with the tandem octarepeats of the mammalian prion protein. Chemistry: A European Journal 20(31), 9770-9783. 10.1002/chem.201304201