Riga / Lie`ge / Uppsala / Warwick / Stockholm / Washington / DC / Pittsburgh / San Diego / Brussels / Sevilla / Meadow / /
Company
HN / Drosophila SA / 15N / Data Bank / Millipore / Amersham / Ge / BioMagResBank / Martek Biosciences Corporation / Pearson / Celera / Elsevier Science Ltd / assigned using 15N / /
Country
Switzerland / Latvia / Sweden / Belgium / United States / United Kingdom / /
Currency
pence / GBP / / /
Facility
Protein Engineering Lie`ge University / Chemistry Australian National University / Biophysics Karolinska Institute / /
IndustryTerm
active site / substrate-binding site / a-amino / metal-binding site / putative zinc-binding site / zinc-coordination site / metal chelators / degradation products / energy / energy refinements / mM solutions / chemical groups / chemical shift degeneracy / Metal content analysis / chemical shifts / lactyl / chemical / chemical microsequencing23 / /
Organization
Research School / Institut Malvoz / Karolinska Institute / American Chemical Society / Swedish Research Council / Department of Medical Biochemistry / Institut de Chimie / Protein Engineering Lie`ge University / Federal Office for Scientific / Technical and Cultural Affaires / Swedish NMR Centre / Australian National University / /
Person
Ha / Van Beeumen / Catherine Ge´ne / Johan Weigelt / Christine Jacobs / Note / Andrew Torda / /
Position
*Corresponding author / Hb / corresponding author / R. N. / associate researcher / /
Product
M-9 / folic acid / /
ProvinceOrState
Alabama / North Dakota / /
PublishedMedium
la Recherche / /
Technology
Protein Engineering / UDP / Sander algorithm / human genome / dielectric / spectroscopy / dialysis / /
doi:[removed]S0022[removed] J. Mol. Biol[removed], 833–842 NMR Structure of Citrobacter freundii AmpD, Comparison with Bacteriophage T7 Lysozyme and