develop a sound strategy for addressing the nation's environmental problems. Research in the molecular sciences will also have far-ranging effects on many other DOE missions, including energy efficiency and national defense. Also, the new approach to collaborative research embodied in the EMSL—which makes full use of the latest advances in computing and communication technologies—will serve as a model for focusing the country's scientific resources on other vital national issues.
I thank Sunney Xie, Michael Kennedy, David Feller, and Robert Harrison for providing the research material discussed here. I dedicate this paper to the memory of William R. Wiley, for his vision and steadfastness, and to Michael L. Knotek, for teaching us how to identify and cope with the myriad issues in establishing the EMSL. Without them, there would not have been an EMSL.
"Ultimately a hero is a man who would argue with the gods, and so awakens the devils to contest his vision."
(special preface to the 1st Berkeley Edition of The Presidential Papers ). I also dedicate this article to the staff of the William R. Wiley Environmental Molecular Sciences Laboratory, in whose hands the future of the EMSL rests.
1. Koomanoff FA. Scientific User Facilities, A National Resource. U.S. Department of Energy, Office of Energy Research, Washington, DC, 1994.
2. Riley RG, Zachara JM, Wobber FJ. Chemical Contaminants on DOE Lands and Selection of Contaminant Mixtures for Subsurface Science Research, U.S. Department of Energy, Office of Energy Research, Washington, DC, 1992 (DOE/ER-0547T).
3. Xie XS. Single molecule spectroscopy and dynamics at room temperature. Accounts of Chemical Research 1996; 29:598—606
4. Xun L, Topp E, Oser, CS. Confirmation of Oxidative Dehalogenation of Pentachlorophenol by a Flavobacterium Pentachlorophenol Hydroxylase. Journal of Bacteriol 1992; 174: 5745-5747.
5. Lu HP, Xun L, Xie XS. Manuscript in preparation.
6. Xue QF, Yeung ED. Difference in the Chemical Activity of Individual Molecules of an Enzyme. Nature 1995; 373: 681-683.
7. Buchko GW, Kennedy MA. Human Nucleotide Excision Repair Protein XPA: 1H NMR and CD Solution Studies of a Synthetic Peptide Fragment Corresponding to the Zinc Binding Domain (101-141). Journal of Biomolecular Structure and Dynamics 1997; 14:677-690.
8. Buchko GW, Ni S, Thrall BD, Kennedy MA. Human Nucleotide Excision Repair Protein XPA: Expression and NMR Backbone Assignments of the 14.7 kD Minimal Damaged-DNA Binding Domain (M98-F219). Journal of Biomolecular NMR 1997; in press.
9. Glendening ED, Feller D, Thompson MA. An Ab Initio Investigation of the Structure and Alkali Metal Cation Selectivity of 18-Crown-6. Journal of the American Chemical Society 1994; 116:10657. [See also, Feller D, Thompson MA, Kendall RA. A Theoretical Study of Substituent Effects on the Binding Specificity of Crown Ethers. Journal of Physical Chemistry 1997; in press.]
10. Anchell J, Apra E, Bernholdt D, Borowski P, Clark T, Clerc D, Dachsel H, Deegan M, Dupuis M, Dyall K, Farm G, Fruchtl H, Gutowski M, Harrison R, Hess A, Jaffe J, Kendall R, Kobayashi R, Kutteh R, Lin Z, Littlefield R, Long X, Meng B, Nichols J, Nieplocha J, Rendall A, Stave M, Straatsma T, Taylor H, Thomas G, Wolinski K, Wong A, NWChem, A Computational Chemistry Package for Parallel Computers, Version 3.0. 1997. Pacific Northwest National Laboratory, Richland, Washington 99352-0999, USA.
11. Li G, Still WC. An 18-Crown-6 Derivative with Only One Conformation. Journal of the American Chemical Society 1993; 115: 3804-3805.
12. Kendall RA, Dunning TH Jr., Harrison RJ. Electron affinities of the fast-row atoms revisited. Systematic basis sets and wave functions. Journal of Chemical Physics 1992; 96: 6796-6806.