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«Department of Physics Phone: 509-527-5229 Program in Biochemistry, Biophysics Fax: 509-527-5904 & Molecular Biology (BBMB) Email: juersdh ...»

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Douglas Henry Juers

Department of Physics Phone: 509-527-5229

Program in Biochemistry, Biophysics Fax: 509-527-5904

& Molecular Biology (BBMB) Email: juersdh@whitman.edu

Whitman College http://www.whitman.edu/~juersdh/

Walla Walla,WA 99362


2000 PhD, Department of Physics, University of Oregon, Eugene, OR. Brian W. Matthews,

Advisor. Dissertation: A Structural View of Beta-Galactosidase in Action 1987 A.B., Department of Physics, Cornell University, Ithaca, NY Professional Positions 2010 - present Associate Professor, Department of Physics and Program in Biophysics, Biochemistry and Molecular Biology, Whitman College.

Courses taught: 20th Century Physics with Lab, Introductory Mechanics Lab, Biophysics with Lab, BBMB Senior Seminar Research projects: Understanding the nature of cooling-induced damage to protein crystals to develop predictive cooling methods. Structural biology studies on dioxygenases (with T.

Machonkin, Chemistry).

Committees: Curriculum Committee, Faculty Athletics Representative, Institutional Review Board, General Studies Committee.

2012 – 2013, 2013 - present Chair, Department of Physics, Whitman College.

2012 - present Interactive Images Editor, Protein Science Work with authors to develop interactive images for manuscripts accepted to Protein Science.

2004 - 2010 Assistant Professor, Department of Physics and Program in Biophysics, Biochemistry and Molecular Biology, Whitman College.

Courses taught: Introductory Mechanics with Lab, Introductory Electricity & Magnetism with Lab, Thermal Physics, 20th Century Physics Lab, Advanced Electricity & Magnetism, Biophysics with Lab.

Research projects: Understanding the nature of cooling-induced damage to protein crystals to develop predictive cooling methods. Structural biology studies on myelin basic protein, PIRL protein (with D. Vernon, Biology), aldehyde dehydrogenase (with J. Russo, Chemistry), and dioxygenases (with T. Machonkin, Chemistry).

Visiting Scientist, Institute de Biologie Structurale, Laboratoire de Biophysique Moléculaire and European Synchrotron Radiation Facility, Grenoble, France Projects: Raman spectroscopic investigations of protein crystal cooling, humidity control of protein crystal cooling, the temperature dependence of protein conformation, the temperature behavior of lipidic cubic phases, and radiation damage to protein crystals.

2000 - 2004 Post-doctoral research fellow, Department of Physics, Howard Hughes Medical Institute and Institute of Molecular Biology. Brian W. Matthews, Advisor.

Studies on long-range order in macromolecular crystals and the catalytic activity of E. coli βgalactosidase.

1993 - 2000 Graduate Research Assistant, Department of Physics, Howard Hughes Medical Institute and Institute of Molecular Biology. Brian W. Matthews, Advisor.

Structural and functional studies on E. coli β-galactosidase and thermolysin.

1988 - 1992 Teacher, coach & dorm parent. Carrabassett Valley Academy, Kingfield, ME.

Extramural Funding Pending “New Predictive Methods for Cryoprotection in Macromolecular Crystallography” (PI).

National Institutes of Health. Amount: $396,851. Award Period: 6/01/15-5/31/18.

“The Sources of Substrate Specificity in Hydroquinone Dioxygenases” (co-PI with T.

Machonkin-PI). National Science Foundation. $399,456. Award Period 2015-18.

Completed “New Predictive Methods for Cryoprotection in Macromolecular Crystallography” (PI).

National Institutes of Health. Award Period: 9/01/10 – 8/31/14.

“MRI: Acquisition of a Laser Scanning Confocal Microscope to Build an Integrative Life Sciences Imaging Program and Create New Research Opportunities at Whitman College” (coDouglas Juers cv 2 of 6 PI with Profs. Withers-PI, Wallace, Vernon, L. Knight, Department of Biology). National Science Foundation. Award Period: 8/15/10 – 8/14/13.

“The Sources of Substrate Specificity in Hydroquinone Dioxygenases” (co-PI with T.

Machonkin-PI). National Science Foundation. Award Period: 4/15/10-5/14/13.

“MRI: Acquisition of an X-ray Diffraction Instrument for Interdisciplinary and Collaborative Research and Education in an Undergraduate Setting”, PI, with J. Russo, D. Vernon, T.

Machonkin & K. Nicolaysen. National Science Foundation. 2007-2010.

Publications - all are peer reviewed except Juers & Matthews (2004), which was a commissioned review. Whitman College students are indicated with an asterisk.

1. Von Stetten, D., Giraud, T., Carpentier, P., Sever, F., Terrien, M., Dobias, F., Juers, D.H., Flot, D., Mueller-Dieckmann, C., Leonard, G.A., de Sanctis, D. & Royant, A. In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF. (2015) Acta Crystallographica D71, 15-26.

2. Matheson, G.R.*, Chang, P.S.*, Rosenbaum, A.*, Juers, D.H. & Juhasz, M.A. Microwaveassisted iodination: synthesis of heavily iodinated 10-vertex and 12-vertex boron clusters (2014) Synthesis and Reactivity in Inorganic, Metal-Organic, and Nano-Metal Chemistry (in press).

3. Juers, D.H. & Ruffin, J.* MAP_CHANNELS: A Computational Tool to Aid in the Visualization and Characterization of Solvent Channels in Macromolecular Crystals. (2014) Journal of Applied Crystallography, 47,2105-2108.

4. Farley, C.* & Juers, D.H. Efficient Cryoprotection of Macromolecular Crystals by Vapor Diffusion of Volatile Alcohols. (2014) Journal of Structural Biology, 188, 102-106.

5. Farley, C.*, Burks, G.*, Siegert, T.* & Juers, D.H. Improved reproducibility of cell parameters in macromolecular cryocrystallography by limiting dehydration during crystal mounting (2014) Acta Crystallographica D70, 2111-2124.

6. Juhasz, M.A., Juers, D.H., Dwulet, G.E.* & Rosenbaum, A.J.* Tetraethylammonium 7,12dicyano-1-carba-closo-dodecaborate (2014) Acta Crystallographica E70, o411-o412

7. Rosenbaum, A.J.*, Juers, D.H. & Juhasz, M.A. Copper-promoted Cyanation of a Boron Cluster:

Synthesis, X-ray structure, and Reactivity of 12-CN-closo-CHB11H10.(2013) Inorganic Chemistry 52: 10717-10719.

8. Juers,D.H., Matthews,B.W. & Huber, R.E. LacZ beta-galactosidase: Structure and function of an enzyme of historical and molecular biological importance. (2012) Protein Science 21:1792-1807.

9. Marshall, H.*, Venkat, M.*, Hti Lar Seng, N.S.*, Cahn, J.*, Juers, D.H. The use of trimethylamine N-oxide as a primary precipitating agent and related methylamine osmolytes as cryoprotective agents for macromolecular crystallography. (2012) Acta Crystallographica D68, 69-81.

10. Russi, S., Juers, D.H., Sanchez-Weatherby, J., Pellegrini, E., Mossou, E., Forsyth, V.T., Gobbo, A., Felisaz, F., Moya, R., McSweeney, S.M., Cusack, S., Cipriani, F., Bowler, M.W. Inducing phase changes in crystals of macromolecules: Status and perspectives for controlled crystal dehydration. (2011) Journal of Structural Biology 175, 236-243.

11. Juers, D. H. & Weik, M. Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin. (2011) J. Synchrotron Rad. 18, 329-337.

12. Coquelle, N., Talon, R., Juers, D.H., Girard, É, Kahn, R. Gradual Adaptive Changes of a Protein Facing High Salt Concentrations. (2010) Journal of Molecular Biology. 404, 493-505.

Douglas Juers cv 3 of 6

13. Alcorn, T.* & Juers, D.H. Progress in Rational Methods of Cryoprotection in Macromolecular Crystallography. (2010) Acta Crystallographica D66, 366-373..

14. Juers, D.H. Rob, B., Dugdale, M., Rahimzadeh, N., Giang, C., Lee, M., Matthews, B.W. & Huber, R.E. (2009) Direct and Indirect Roles of His-418 in Metal Binding and in the Activity of β-Galactosidase (E. coli). Protein Science. 18:1281-1292.

15. Juers, D.H., Lovelace, J., Bellamy, H.D., Snell, E.H., Matthews, B.W. and Borgstahl, G.E.O.

(2007) Changes to Crystals of E. coli β-galactosidase During Room-Temperature LowTemperature Cycling and Their Relation to Cryo-Annealing. Acta Crystallographica. D63, 1139Juers, D.H., Kim J., Sieburth, S. McN., and Matthews, B.W. Structural Analysis of Silendiols as Transition-State-Analogue Inhibitors of the Benchmark Metalloprotease Thermolysin. (2005) Biochemistry 44, 16524-16528.

17. Juers, D.H. and Matthews, B.W. Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization. (2004) Quarterly Reviews of Biophysics 37, 2 pp. 1-15. Review commissioned to BWM.

18. Juers, D.H. and Matthews, B.W. (2004) The Role of Solvent Transport in Macromolecular Crystal Annealing. Acta Crystallographica, D60, 412-421.

19. Juers, D.H., Hadka, S., Matthews, B.W., and Huber, R.E. (2003) The Structural Basis for the Altered Activity of Gly 794 Variants of E. coli β-Galactosidase. Biochemistry 42: 13505-13511.

20. Shoemaker, G.K., Juers, D.H., Coombs, J.M.L., Matthews, B.W. and Craig, D.B. (2003) Crystallization of β-Galactosidase Does Not Reduce the Range of Activity of Individual Molecules. Biochemistry 42: 1707-1710.

21. Juers, D.H., Heightman, T.D., Vasella, A., McCarter, J.D., Mackenzie, L., Withers, S.G. and Matthews, B.W. (2001) A Structural View of the Action of E. coli (lac Z) β-Galactosidase.

Biochemistry 40: 14781-14794.

22. Juers, D.H. and Matthews, B.W. (2001) Reversible Lattice Repacking Illustrates the Temperature Dependence of Macromolecular Interactions. Journal of Molecular Biology 311 851-862.

23. Juers, D.H., Jacobson, R.H., Wigley, D., Zhang, X.J., Huber, R.E., Tronrud, D.E. and Matthews, B.W. (2000) High resolution refinement of β-galactosidase in a new crystal form reveals multiple

metal-binding sites and provides a structural basis for α-complementation. Protein Science 9:


24. Juers D.H., Huber, R.E. and Matthews, B.W. (1999) Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β-galactosidase and other glycohydrolases. Protein Science 8:122-136.

25. Holland, D.R., Hausrath, A.C., Juers, D.H. and Matthews B.W. (1995) Structural analysis of zinc substitutions in the active site of thermolysin. Protein Science 4: 1955-1965.

Provisional Patent Application No. 62/015,186. System to Control the Local Humidity of a Sample During Manipulation Under Microscope and Subsequent Transfer to an Analytical Instrument. Filed: June 20, 2014.

Douglas H. Juers & Christopher A. Farley Invited Lectures

1. Macromolecular Crystallography 1914-2014 with Differential Diffusion as a Root Cause of Cracking in Protein Crystals. Annual Meeting of the Northwest Section of the American Physical Society, University of Washington, May, 2014.

Douglas Juers cv 4 of 6

2. Proteins, Powders and Small Molecules – Multidisciplinary Uses of X-ray Diffraction at an Undergraduate Institution. Annual Meeting of the American Crystallographic Association, Boston, MA, Aug 2012.

3. Multidisciplinary Uses of X-ray Diffraction with an Xcalibur Nova. Agilent Luncheon. Annual Meeting of the American Crystallographic Association, Boston, MA, Aug 2012.

4. Lessons from Ocean Going Organisms - Stabilizing Osmolytes as Tools for Protein Crystallography. Chemistry Department Seminar, Reed College, Portland, OR. February, 2012.

5. Stabilizing Osmolytes as Agents of Crystal Growth and Cryoprotection in Macromolecular Crystallography. Chemistry Department Seminar, Gonzaga University, Spokane, WA. October, 2011.

6. Rational Approaches to Crystal Cooling. CCP4 Study Weekend. Nottingham, UK. January, 2009.

7. Rational Approaches to Cryocrystallography. Gordon Conference: Diffraction Methods in Structural Biology. Bates College, Lewiston, Maine. July, 2008.

8. The Role of Cryoprotectants in the Successful Cooling of Protein Crystals. 10th Annual Meeting of the Northwest Section of the American Physical Society. Lewis & Clark College, Portland, OR. May, 2008.

The Role of Water Transport in Cryo-Annealing. Lecture. Annual Meeting of the American 9.

Crystallographic Association, Cincinnati, OH June 2003.

Other Presentations

1. Improved Reproducibility of Cell Parameters in Macromolecular Cryocrystallography by Limiting Dehydration During Crystal Mounting. Juers, DH. Northwest Crystallography Workshop, Oregon State University, Corvallis, OR. July 2014.

2. Improved Cell Parameter Reproducibility in Macromolecular Cryo-Crystallography. Farley, CA* & Juers DH. Biophysical Society Annual Meeting, San Francisco, CA. February, 2014.

3. A Computational Tool for Characterizing Solvent Channels in Macromolecular Crystals. Juers DH, Saxby C*, Cahn J*, Venkat M*. Poster. Protein Society Annual Meeting, Boston, MA, July, 2013. Northwest Crystallography Workshop, Montana State University, Bozeman MT.

July 2012.

4. Thermal Contraction Guided Cryoprotectant Selection. Saxby C*, Cahn J*, Venkat M*, Juers DH. Poster. Northwest Crystallography Workshop, Montana State University, Bozeman, MT.

July 2012.

5. Investigations of the Stabilizing Osmolyte, TMAO, as a New Precipitant for Protein Crystallization. Marshall H*, Venkat M*, Juers D. Poster. Annual Meeting of the Northwest American Physical Society, Whitman College, Walla, Walla WA. October, 2010.

6. A Time and pH-Dependent Conformational Change in MntR Crystals. Cahn J*, Glasfeld A, Juers DH. Poster. Northwest Crystallography Workshop, University of British Columbia, Vancouver, BC. June 2010

7. Slow Cooling, Radiation Damage and Annealing in Crystals of Thermolysin, Juers DH & Weik.

M. Seminar. 6th International Conference on Radiation Damage to Crystalline Biological Samples, Stanford Synchrotron Radiation Laboratory, March 2010.

8. Towards Rational Methods of Cryoprotectant Choice in Macromolecular Crystallography, Institute de Biologie Structurale, Grenoble, France, April 2009.

9. Physical Properties of Cryoprotective Solutions for Macromolecular Crystallography. Poster.

Frontiers in Microrheology Workshop, UCLA, Los Angeles, CA, Feb 2008.

10. Ibid. Poster. 52nd Annual Meeting of the Biophysical Society, Long Beach, CA, Feb 2008.

Douglas Juers cv 5 of 6

11. Hysteresis in Cryo-Cooling Crystals of E. coli β−galactosidase and its Relations to CryoAnnealing. Poster. 51st Annual Meeting of the Biophysical Society, Baltimore, MD, March 2007.

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