Protein crystal structure analysis from high-resolution X-ray powder-diffraction data.
Although high-resolution powder diffraction of proteins is in its infancy, we can easily see future developments of the method that will allow examination of protein structures that exceed 100 kDa. In particular, current data-collection technology scans the powder-diffraction pattern a few points at a time over a very narrow field of view. The use of high-resolution imaging technology and X-ray focusing optics should improve this 1000-fold or more, making it possible to use powder diffraction on a laboratory X-ray source to screen for the formation of protein/drug complexes and to determine their structures.
Von Dreele
Robert B
RB
Los Alamos National Laboratory, Lujan Center, Los Alamos, New Mexico 87545, USA.
D000818:Animals; D002645:Chickens; D018360:Crystallography, X-Ray / Q000379:methods; D007328:Insulin / Q000737:chemistry; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D033362:Powder Diffraction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D014961:X-Ray Diffraction / Q000379:methods
D007328:Insulin; D011506:Proteins; D009113:Muramidase