A dilute solution parameter obtained from static light-scattering measurements is proposed as a predictor for protein crystallization experiments. The osmotic second virial coefficients, B22, have been measured for a variety of proteins in solvents that are known to promote crystallization and the values for B22 were found to lie within a fairly narrow range which we refer to as a crystallization slot. Solution conditions which were known not to favor crystallization of the proteins resulted in B22 values well outside the crystallization slot.

Only the third known example of a homoleptic polynitrogen species besides N2 and N3−, the N5+ ion possesses surprising stability and can be isolated on a macroscopic scale as its AsF6− salt. The assigment of the C2v‐symmetric structure (shown schematically) predicted by calculations was supported by IR and Raman as well as 14N and 15N NMR spectroscopic studies of the isotopically labeled product.

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