Articles

Crystallography Illuminates Drug Targets
James Netterwald, PhD, MT(ASCP), Senior Editor, Drug Discovery & Development,

Knowing the structure of a protein used to be of greater importance to basic biological science than to applied biomedical science. However, as these fields converge, knowing and understanding protein structure has become imperative for both. X-ray crystallography, the most important tool for determining protein structure, is the preeminent tool of the relatively new science of structural biology, but its use in science in general is not new at all.

Immunoglobulin Cross-Reactivity Examined by Library Screening, Crystallography and Docking Studies
Ramsland P.A., Yuriev E. and Edmundson A.B., Oklahoma Medical Research Foundation

Antibodies are extremely diverse with respect to their specificities and affinities for target molecules. Despite rigorous selection, some antibodies are cross-reactive whereby they recognize their natural antigens along with other molecules. In this review, we discuss our efforts toward understanding the cross-reactivity of selected immunoglobulins. Investigations that are discussed employed screens of combinatorial peptide libraries, crystallography of ligand-protein complexes, and computer-ba

Recent Advances in Atomic Resolution Protein Crystallography
Luciana Esposito, Luigi Vitagliano and Lelio Mazzarella, Istituto di Biostrutture e Bioimmagini and Dipartimento di Chimica

In the search for increasingly accurate protein structures, technological advances are opening up new possibilities. In the last few years the wide accessibility of intense synchrotron sources, the availability of efficient 2D-detectors, and the routine use of cryo-crystallography techniques have yielded a significant number of atomic resolution protein structures. Here we review the most interesting results achieved in this field with a particular emphasis to the biological implications and to

Optimizing Buffers for Protein Purification using Dynamic Light Scattering
Ulf Nobbmann (Malvern Instruments, Malvern, UK,) Muriel Uhring, Aurélie Martinez and Jean-Paul Renaud (AliX, Illkirch, France), Malvern Instruments and AliX

A proprietary material, ProteinT, failed to crystallize in the initial preparation and test buffer. The formulation was subsequently changed and improved conditions were determined with the aid of dynamic light scattering. The resultant buffer choice was selected for overnight dialysis and resulted in improved protein purification.