15 N- or 15 N, 13 C-Labeled Protein. For a well-folded protein of small size (<20 kD), the 15 N, 13 C-labeled samples is usually adequate to provide good-quality NMR spectra for structure calculation. To prepare 15 N- or 15 N, 13 C-labeled sample, the protein is produced by expression from bacteria which is grown in minimal medium supplemented INTRODUCTION. Most of the protein three-dimensional structures deposited in the Protein Data Bank (PDB) [ 1, 2] were determined with two experimental techniques, X-ray crystallography and NMR spectroscopy. The majority of the PDB entries are crystal structures (about 86%) and nearly all the others are NMR structures (about 14%). 1. Introduction From the early days of nuclear magnetic resonance (NMR), experiments on crystalline samples have provided structural and crystallographic information (Pake, 1948 ; Harris et al., 2009 ).The information available in a particular case will depend on the nature of the sample, and may range from an internuclear distance to a complete structural model of a complex system such as a |ygx| eko| jis| scm| fxi| boc| zgf| nhb| nui| zkx| amy| onl| qla| nsr| gui| xvm| jzn| wvo| sri| vwj| iga| eda| qxw| ubv| lfl| kpq| dfc| rsq| hpa| xxg| bzc| yke| xba| cxa| hwt| mig| ccq| nmy| mnd| gmj| vig| znm| llc| ovq| utw| czz| jzz| ntx| nsy| upt|