My research interests include developing new methods for crystallization of biomolecules, new methods for detection of nanocrystals, and new methods for in situ X-ray data collection.
At the Crystallization Center, we provide high-throughput screening for biomolecules to determine initial crystallization conditions, working with scientists around the world (www.getacrystal.org).
My research lab is interested in developing new methods that combine crystallographic and spectroscopic approaches to answer fundamental questions about protein biochemistry, especially in proteins that contain metals. We are working to develop spectroscopic methods for single crystals (electron paramagnetic resonance, UV-visible microspectrophotometry, and energy dispersive X-ray spectroscopy for elemental analysis) to be used in parallel with crystallography. My lab is especially interested in investigating proteins that are important in cancer and in neurodegenerative diseases.
Our commitment to diversity
The Bowman Lab welcomes members regardless of race, religion, gender identification, sexual orientation, age, or disability status.
Welcome to Yana Shimanovich!
Yana has joined the Bowman and Snell Labs for her MDI Master’s degree! Welcome!
Good luck in grad school Ethan!
Ethan did a fantastic job with a new GUI for MARCO automated classification of crystal images! Beta version will be available soon. He is on his way to graduate school at UC Davis!
Screening for SARS-CoV-2 protein crystals!
Screening for crystal growth of SARS-CoV-2 related samples at the Crystallization Center and getting great results!
Dr. Jeney Wierman, Dr. Jennifer Bridwell-Rabb and I are organizing a workshop for the 2020 SSRL/LCLS Users’ Meeting on Metals in Structural Biology!
Interviewed on Spectrum News!
See the story about our work in the Crystallization Center on SARS-CoV-2!
Lynch, ML, Dudek, MF, Bowman, SEJ. A Searchable Database of Crystallization Cocktails in the PDB: Analyzing the Chemical Condition Space. Patterns 2020; 1(4), 100024.
Bowman, SEJ, Backman, LRF, Bjork, RE, Andorfer, MC, Yori, S, Caruso, A, Stultz, CM, Drennan, CL. Solution structure and biochemical characterization of a spare part protein that restores activity to an oxygen-damaged glycyl radical enzyme. Journal of Biological Inorganic Chemistry (2019). 24:817.
Nakashige, TG, Bowman, SEJ, Zygiel, EM, Drennan, CL, Nolan, EM. Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and His3Asp Site. Biochemistry, 2018; 57(28):4155-4164.
Bowman, SEJ*, Bridwell-Rabb, J*, Drennan, CL. Metalloprotein crystallography: More than a structure. Acc Chem Res. 2016 Apr 19;49(4):695-702.
*denotes co-first author publication.
ACS Editors’ Choice Article
Featured on journal cover
Gagnon, DM, Brophy, MB, Bowman, SEJ, Stich, TA, Drennan, CL, Britt, RD, Nolan, EM. Manganese binding properties of human calprotectin under conditions of high and low calcium: X-ray crystallographic and advanced electron paramagnetic resonance spectroscopic analysis. J Am Chem Soc. 2015 Mar 4;137(8):3004-16.
Galinato, MGI, Bowman, SEJ, Kleingardner, JG, Martin, S, Zhao, JY, Sturhahn, W, Alp, EE, Bren, KL, Lehnert, L. Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c. Biochemistry. 2015 Feb 3;54(4):1064-76.
Kleingardner, JG, Bowman, SEJ, Bren, KL The influence of heme ruffling on porphyrin spin densities in cytochromes c probed by core heme carbon NMR. Inorg Chem. 2013 Nov 18;52(22):12933-46.
Galinato, MGI, Kleingardner, JG, Bowman, SEJ, Alp, EE, Zhao, J, Bren, KL, Lehnert, N. Heme-protein vibrational couplings in cytochromes c provide a dynamic link that connects the heme-iron and the protein surface. Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):8896-900.
Levin, BD, Can, M, Bowman, SEJ, Bren, KL, Elliott, SJ. Methionine ligand lability in bacterial monoheme cytochromes c: An electrochemical study. J Phys Chem B. 2011 Oct 13;115(40):11718-26.
Chung, JK, Thielges, MC, Bowman, SEJ, Bren, KL, Fayer, MD. Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments. J Am Chem Soc. 2011 May 4;133(17):6681-91.
Bowman, SEJ, Bren, KL. Variation and analysis of second sphere interactions and axial histidinate character in c-type cytochromes. Inorg Chem. 2010 Sep 6;49(17):7890-7
Bowman, SEJ, Bren, KL. The chemistry and biochemistry of heme c: Functional bases for covalent attachment. Nat Prod Rep. 2008 Dec;25(6):1118-30. doi: 10.1039/b717196j.
Kim, S, Chung, JK, Kwak, K, Bowman, SEJ, Bren, KL, Bagchi, B, Fayer, MD. Native and unfolded cytochrome c – Comparison of dynamics using 2D-IR vibrational echo spectroscopy. J Phys Chem B. 2008 Aug 14;112(32):10054-63.
Michel, LV, Ye, T, Bowman, SEJ, Levin, BD, Hahn, MA, Russell, BS, Elliott, SJ, Bren, KL. Heme attachment motif mobility tunes cytochrome c redox potential. Biochemistry. 2007 Oct 23;46(42):11753-60.
2019 BioXFEL Intern Current: UC Berkeley Graduate Student in Computational Biology
2018 HWI Intern
Current: University of Pittsburgh undergraduate
Summer 2018 Interns
Summer 2019 Interns
Maid of the Mist
- Cornell College, English Literature and Women’s Studies BSS
- Metropolitan State College of Denver, Chemistry, BS
- University of Rochester, Chemistry, MS, PhD
- Massachusetts Institute of Technology, Postdoc
- Los Alamos National Laboratory, Postdoc