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.

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:

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!

Selected Publications

Google Scholar Profile

orcid.org/0000-0002-7426-7328

Budziszewski, GR, Snell, ME, Wright, TR, Lynch, ML, Bowman, SEJ. High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography. J. Vis. Exp. 2023, (193), e65211.

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.

Chattopadhyay, S, Mukherjee, M, Kandemir, B, Bowman, SEJ, Bren, KL, Dey, A. Contributions to Cytochrome c Inner- and Outer-Sphere Reorganization Energy. Chemical Science, 2021, 12: 11894-913.

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.

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.

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.

Education