Heat capacity and phase equilibria of hollandite polymorph of KAlSi 3 O 8

The low-temperature heat capacity ( C p ) of KAlSi 3 O 8 with a hollandite structure was measured over the range of 5–303 K with a physical properties measurement system. The standard entropy of KAlSi 3 O 8 hollandite is 166.2±0.2 J mol −1  K −1 , including an 18.7 J mol −1  K −1 contribution from the configurational entropy due to disorder of Al and Si in the octahedral sites. The entropy of K 2 Si 4 O 9 with a wadeite structure (Si-wadeite) was also estimated to facilitate calculation of phase equilibria in the system K 2 O–Al 2 O 3 –SiO 2 . The calculated phase equilibria obtained using Perple_x are in general agreement with experimental studies. Calculated phase relations in the system K 2 O–Al 2 O 3 –SiO 2 confirm a substantial stability field for kyanite–stishovite/coesite–Si-wadeite intervening between KAlSi 3 O 8 hollandite and sanidine. The upper stability of kyanite is bounded by the reaction kyanite (Al 2 SiO 5 ) = corundum (Al 2 O 3 )  + stishovite (SiO 2 ), which is located at 13–14 GPa for 1,100–1,400 K. The entropy and enthalpy of formation for K-cymrite (KAlSi 3 O 8 ·H 2 O) were modified to better fit global best-fit compilations of thermodynamic data and experimental studies. Thermodynamic calculations were undertaken on the reaction of K-cymrite to KAlSi 3 O 8 hollandite +  H 2 O, which is located at 8.3–10.0 GPa for the temperature range 800–1,600 K, well inside the stability field of stishovite. The reaction of muscovite to KAlSi 3 O 8 hollandite + corundum + H 2 O is placed at 10.0–10.6 GPa for the temperature range 900–1,500 K, in reasonable agreement with some but not all experiments on this reaction.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/46910/1/269_2006_Article_63.pd

Mechanistic insights into the recycling machine of the SNARE complex

Evolutionarily conserved SNARE (Soluble N-ethylmaleimide sensitive factor Attachment protein REceptors) proteins form a complex that drives fusion between membranes in eukaryotes. SNARE complexes are disassembled by the ATPase NSF (N-ethylmaleimide Sensitive Factor), together with SNAP (Soluble NSF Attachment Protein) proteins, making individual SNAREs available for a subsequent round of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometer resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains, to pseudo four-fold symmetry of the SNARE complex. SNAPs are interacting with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes