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X-ray crystallography is still the primary method for characterizing the atomic structure of materials and in differentiating materials that appear similar in other experiments. X-ray crystal structures can also help explain unusual electronic or elastic properties of a material, shed light on chemical interactions and processes, or serve as ...
Two forces converged to initiate the PDB: a small but growing collection of sets of protein structure data determined by X-ray diffraction; and the newly available (1968) molecular graphics display, the Brookhaven RAster Display (BRAD), to visualize these protein structures in 3-D.
From 1965, the group began to collect published bibliographic, chemical and crystal structure data for all small molecules studied by X-ray or neutron diffraction. With the rapid developments in computing taking place at this time, this collection was encoded in electronic form and became known as the Cambridge Structural Database (CSD).
X-ray crystallography is one of the essential components in bubblegram imaging as it is the process of how X-ray radiation is used to identify structures and surfaces of specimens. The electromagnetic radiation emitted is from the charged electrons being controlled to reveal the patterns formed by the protein.
"An Intersection Function and Its Relations to the Minimum Function of X-Ray Crystallography". Proceedings of the National Academy of Sciences of the United States of America. 39 (7): 678–80. doi: 10.1073/pnas.39.7.678. PMC 1063844. PMID 16589324. Buerger MJ (February 1954). "Some Relations for Crystals with Substructures".
(Molecules need to crystallize into solids so that their regularly repeating arrangements can be taken advantage of in X-ray, neutron, and electron diffraction based crystallography). Crystal structures of crystalline material are typically determined from X-ray or neutron single-crystal diffraction data and
David Sayre (March 2, 1924 – February 23, 2012) was an American scientist, credited with the early development of direct methods for protein crystallography and of diffraction microscopy (also called coherent diffraction imaging).
Early demonstrations of isomorphous replacement in crystallography come from James M. Cork, [3] John Monteath Robertson, [4] and others. An early demonstration of isomorphous replacement in crystallography came in 1927 with a paper reporting the x-ray crystal structures of a series of alum compounds from Cork. [3]