The Bowman Lab
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. 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.
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).
Software and scripting developed in the Bowman Lab are available on GitHub.
Our commitment to diversity
The Bowman Lab welcomes members regardless of race, religion, gender identification, sexual orientation, age, or disability status.
Bowman Lab News!
New NIH Research Funding!
We are excited to announce that the Bowman Lab has received our first R01 grant from NIH!
In this MPI project with Dr. Miranda Lynch, we will develop innovative technologies for both image analysis and sample handling expressly designed to address the speciﬁc challenges of working with very small crystals. These innovations will be a powerful addition to the structural biology toolbox for leveraging the cutting edge diffraction based methods available for structure determination.
Luz Alfaro will be joining NIH NCI for a post-baccalaureate research position after graduating from Grinnell College! Congrats!
New perspective article about the role of structural biology in the fight against COVID-19!
In the midst of COVID-19, it has been awe-inspiring to see the response of the scientific community, including structural biologists. The IUCrJ perspective is a snapshot of the amazing work by the structural biology community in the past year using X-ray crystallography and cryoEM. Excited to collaborate with Eddie Snell and Miranda Lynch on this piece!
Congratulations to Max!
Max Dudek has been awarded a prestigious 2021 NSF Graduate Research Fellowship award to pursue graduate work! He will be joining the Genomics and Computational Biology PhD prgram at UPenn!
Ethan’s paper is out!
Our new paper implementing MARCO automated crystal scoring is out in Journal of Applied Crystallography! Great work, Ethan!
Code is open-source and available in GitHub! Check out the links below:
Interviewed on Spectrum News!
See the story about our work in the Crystallization Center on SARS-CoV-2!
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!
Miller, RD, Iinishi, A, Modaresi, SM, Yoo, B-K, Curtis, TD, Lariviere, PJ, Liang, L, Son, S, Nicolau, S, Bargabos, R, Morrissette, M, Gates, MF, Pitt, N, Jakob, RP, Rath, P, Maier, T, Mayutin, AG, Kaiser, JT, Niles, S, Karavas, B, Ghiglieri, M, Bowman, SEJ, Rees, DC, Hiller, S, Lewis, K. Computational identification of a systemic antibiotic for gram-negative bacteria. Nat Microbiol. 2022, 7(10):1661-1672.
Lynch, ML, Snell, EH, Bowman, SEJ. Structural biology in the time of COVID-19: perspectives on methods and milestones. IUCrJ 2021; 8, 3, 335-341.
Holleman, ET, Duguid, E, Keefe, LJ, Bowman, SEJ. Polo: an open-source graphical user interface for crystallization screening. Journal of Applied Crystallography, 2021; 54(2):673-679.
Westerman, EL, Bowman, SEJ, Davidson, B, Davis, MC, Larson, ER, Sanford, C. Deploying Big Data to Crack the Genotype to Phenotype Code. Integrative and Comparative Biology, 2020; 60(2):385-396.
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.
Students in the Bowman Lab
Luz Alfaro Summer BioXFEL 2021
Current: Graduating from Grinnell College
Students in the Bowman Lab
Master’s Materials Design and Innovation UB 2020
Summer 2018 Interns
Summer 2019 Interns
Maid of the Mist
- NIH NIGMS R01
- Dr. Louis Skarlow Memorial Trust
- NIH NIGMS R24
- 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