highly ordered structures, such as virus particles. More asymmetrical targets required a return to crystallography, with images captured at various angles from highly ordered 2D crystals that lock the target in a defined orientation. This electron crystallography approach allowed Henderson’s group to produce the first atomic-resolution protein structure solved by EM, of the lightresponsive prot...

Thermolysis of a 1 : mixture tris(di-tert-butylmethylsilyl)germane 9 and bis(di-tert-butylmethylsilyl)germane 17 at 100 °C produces unexpectedly octagermacubane 18, having two 3-coordinate Ge0 atoms (40 % yield). 18 was characterized by X-ray crystallography it is singlet biradical (according to DFT quantum mechanical calculations the absence an EPR signal). Reactions with CH2Cl2 H2O yield nove...

The title compound was synthesized in near-quantitative yield using nucleophilic aromatic substitution of 4,4′-(hexafluoroisopropylidene)diphenol (BPAF) with perfluoropyridine (PFP). purity and structure were determined by NMR (1H, 13C, 19F), GC–EIMS, single-crystal X-ray crystallography.

X-Ray diffraction is the only method currently available for the determination of the detailed three-dimensional structure of macromolecules. In this article, the principles behind the use of X-ray crystallography in the study of protein structure are presented. The results obtained in its application to several enzymes are discussed, as well as the limitations of the method.

The host-guest interaction of a series of cyclohexyl-appended guests with cucurbit[8]uril (Q[8]) was studied by ¹H NMR spectroscopy, isothermal titration calorimetry (ITC), and X-ray crystallography. The X-ray structure revealed that two cycloalkane moieties can be simultaneously encapsulated in the hydrophobic cavity of the Q[8] host to form a ternary complex for the first time.