We investigated the relative distributional persistence of Golgi ‘matrix’ proteins and glycosyltransferases to an endoplasmic reticulum exit block induced by expression of a GDP‐restricted Sar1p. HeLa cells were microinjected with plasmid encoding the GDP‐restricted mutant (T39N) of Sar1p to block endoplasmic reticulum exit and then scored for the distribution of GM130 (Golgi matrix protein of 130 kDa), a cis located golgin; p27, a member of the p24 family of proteins; giantin, a protein that interacts indirectly with GM130; and the Golgi glycosyltransferase, N‐acetylgalactosaminyltransferase‐2 (GalNAcT2). All of these proteins lost their compact, juxtanuclear distribution and displayed characteristics of endoplasmic reticulum/cytoplasmic accumulation with the same dependence on plasmid concentration. The kinetics of redistribution of GM130 and GalNAcT2 were identical. Expression of Sar1pT39N displaced the COPII coat protein Sec13p from endoplasmic reticulum exit sites consistent with disruption of these sites. This occurred without disturbing the overall distribution of endoplasmic reticulum membrane. Furthermore, the reassembly of a juxtanuclear Golgi matrix as assayed by the distribution of GM130 following washout of the Golgi disrupting drug, brefeldin A, was blocked by microinjected Sar1pT39N plasmids. We conclude that the persistence, i.e. stability and maintenance, of Golgi matrix distribution and its reassembly following drug disruption are exquisitely dependent on Sar1p activity.

An algorithm is described for reconstructing a symmetric three-dimensional image from its Fourier intensity that is sampled below the Nyquist rate. The study is motivated by an image reconstruction problem in macromolecular x-ray crystallography. Application of the algorithm to simulated crystallographic problems shows that it converges to the correct solution, with no initial phase information, where algorithms currently used in crystallography fail. The algorithm is potentially useful in a variety of situations in macromolecular crystallography. The results presented also lend support to the possibility of ab initio phase retrieval in macromolecular crystallography when sufficient a priori information is available. Other applications in image reconstruction are possible.

When a surface is placed in a vapor, several layers of molecules may adsorb depending on the intermolecular forces involved. As two such surfaces are brought together, a critical point is reached at which the gas condenses between the surfaces, forming a capillary across the gap. A cohesive force is associated with the condensed bridge. The reverse process wherein the capillary bridge degenerates as the surfaces are moved apart is called snap-off. These processes play a profound role on scales from the nano to the macro. We have studied this phenomenon via isostrain grand canonical Monte Carlo statistical mechanical simulations for Lennard-Jones fluids. Specifically, we have examined capillary condensation and snap-off between nanocontacts, infinite rectilinear nanowires, and finite rectilinear nanoplatelets, where macroscale concepts and theories are just about impossible to apply. These results are compared to condensation between infinite parallel plates. We discuss our results in terms of the Kelvin equation and van der Waals film-thickening model.