Direct Phase Determination in Protein Electron Crystallography: Aquaporin Channel-Forming Integral Membrane Protein

1998 ◽  
Vol 54 (4) ◽  
pp. 615-621 ◽  
Author(s):  
Douglas L. Dorset ◽  
Bing K. Jap
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Electron Crystallography ◽  
Phase Determination

scholarly journals Structural Studies of the Integral Membrane Protein Human LTC4 Synthase by Electron Crystallography

2010 ◽  
Vol 98 (3) ◽  
pp. 647a
Author(s):  
Frederik Rudolph ◽  
Stefania Mari ◽  
Gengxiang Zhao ◽  
Matthew C. Johnson ◽  
Yoshihide Kanaoka ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Structural Studies ◽  
Electron Crystallography

Direct phase determination in electron crystallography: small organic molecules

1992 ◽  
Vol 50 (2) ◽  
pp. 1166-1167
Author(s):  
Douglas L. Dorset
Keyword(s):  
Organic Molecules ◽  
Data Sets ◽  
Temperature Structure ◽  
3D Analysis ◽  
Intensity Data ◽  
Electron Crystallography ◽  
Phase Determination ◽  
Measured Intensity ◽  
3D Data

The quantitative use of electron diffraction intensity data for the determination of crystal structures represents the pioneering achievement in the electron crystallography of organic molecules, an effort largely begun by B. K. Vainshtein and his co-workers. However, despite numerous representative structure analyses yielding results consistent with X-ray determination, this entire effort was viewed with considerable mistrust by many crystallographers. This was no doubt due to the rather high crystallographic R-factors reported for some structures and, more importantly, the failure to convince many skeptics that the measured intensity data were adequate for ab initio structure determinations.We have recently demonstrated the utility of these data sets for structure analyses by direct phase determination based on the probabilistic estimate of three- and four-phase structure invariant sums. Examples include the structure of diketopiperazine using Vainshtein's 3D data, a similar 3D analysis of the room temperature structure of thiourea, and a zonal determination of the urea structure, the latter also based on data collected by the Moscow group.

scholarly journals Predicting the Structure and Dynamics of Membrane Protein GerAB from Bacillus subtilis

2021 ◽  
Vol 22 (7) ◽  
pp. 3793
Author(s):  
Sophie Blinker ◽  
Jocelyne Vreede ◽  
Peter Setlow ◽  
Stanley Brul
Keyword(s):  
Bacillus Subtilis ◽  
Membrane Protein ◽  
Spore Germination ◽  
Structural Information ◽  
Transmembrane Protein ◽  
Homology Modelling ◽  
Water Channel ◽  
Md Simulations ◽  
Integral Membrane Protein ◽  
Starting Point

Bacillus subtilis forms dormant spores upon nutrient depletion. Germinant receptors (GRs) in spore’s inner membrane respond to ligands such as L-alanine, and trigger spore germination. In B. subtilis spores, GerA is the major GR, and has three subunits, GerAA, GerAB, and GerAC. L-Alanine activation of GerA requires all three subunits, but which binds L-alanine is unknown. To date, how GRs trigger germination is unknown, in particular due to lack of detailed structural information about B subunits. Using homology modelling with molecular dynamics (MD) simulations, we present structural predictions for the integral membrane protein GerAB. These predictions indicate that GerAB is an α-helical transmembrane protein containing a water channel. The MD simulations with free L-alanine show that alanine binds transiently to specific sites on GerAB. These results provide a starting point for unraveling the mechanism of L-alanine mediated signaling by GerAB, which may facilitate early events in spore germination.

Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein fromEscherichia coli

1998 ◽  
Vol 54 (4) ◽  
pp. 697-699 ◽  
Author(s):  
Barbara S. Smith ◽  
Bostjan Kobe ◽  
Ravi Kurumbail ◽  
Susan K. Buchanan ◽  
Lalitha Venkatramani ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
X Ray ◽  
Fromescherichia Coli
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