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Timeofflight neutron powder diffraction study on the third row transition metal hexafluorides WF6, OsF6, and PtF6The adiabatic electron affinities (EAs) ofMF 6 and MF; (M = Cr, Mo, and W) are calculated in a configuration interaction (CI) calculation using a model potential method. The calculated EA of 3.85 e V for WF 6 agrees well with the observed values. The difference (1.52 eV) between the calculated EA of MoF6 and that ofWF 6 shows also a very good agreement with the experimental ones. CrF6 has a very high EA of 8.24 eV. The CrF 6 -anion has positive EA and the CrF~dianion is thus most stable in the CrF~-(q = 0, 1, and 2) sequence, while WF; does not have a positive EA. The EAs of MF 6 calculated by CI calculations are smaller than those by SCF calculations. This negative correlation effect on the AEs is also discussed.

Glycoprotein C (gC) of herpes simplex virus type 1 (HSV-1) is a receptor for the complement component C3b. We have previously isolated HSV-1 gC-strains (TN1, TN2 and TN3) from a patient with recurrent keratitis at three different times. These are very rare isolates because gC was thought to be essential for the virus in vivo. To determine whether gC modifies the interaction of complement with cell-free virus or virusinfected cells, we constructed gC + recombinant viruses in which the intact gC gene of strain KOS was inserted into the TN 1 virus genome. TN 1 virus was inactivated by complement and TN1 virus-infected cells were lysed by complement; however, gC ÷ recombinant viruses became resistant to these effects of complement. These results suggest a role for gC in protection of both the virion envelope and the infected cell surface against damage by complement. TN1 virus was inactivated by complement from rats (Wistar, WKA, F344 and SD), guinea-pigs (Hartley) and humans, but not by complement from mice (C3H, DDD and BALB/c), which indicates that mice seem to be inappropriate as an experimental model for the study of HSV infection in which complement factors need to be considered.