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12 citations found for Kuhlbrandt, W.

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The cryo-EM structure of Neurospora crassa respiratory complex IV was determined to 5.5 Å resolution and is compared with related structures from Saccharomyces cerevisiae and Bos taurus.

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Optimized protocols for protein production and purification as well as cryoEM grid preparation allow the reconstruction of a 3D map of yeast fatty acid synthase (FAS) at ∼3 Å resolution from a comparatively small number of particle images within a short time. The first complete model of yeast FAS is presented.

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The N-terminal domain of FeoB from Methanococcus jannaschii was overproduced, purified to homogeneity and crystallized in the presence of GTP and magnesium.

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Acta Cryst. (1996). A52, C140
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Acta Cryst. (2014). A70, C1064
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Na+/H+ antiporters are essential secondary-active transporters that are found across all biological kingdoms and play a crucial role in the pH, sodium and cell volume homeostasis. MjNhaP1 is an archaeal electroneutral Na+/H+-antiporter resembling the human NHE1 exchanger. Substrate-induced conformational changes in MjNhaP1 were examined by electron crystallography of 2D crystals in a range of physiological pH and Na+ conditions. In the absence of sodium, changes in pH had no major effect on the structure of MjNhaP1, whereas changes in Na+ concentration caused a marked conformational change that was largely pH-independent. Crystallographically determined, apparent dissociation constants indicated ~10-fold stronger Na+ binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site. In conjunction with a new 3D EM map of MjNhaP1 a model for transport mechanism is proposed. Conformational changes occur in the 6-helix bundle region of MjNhaP1 that is thought to harbour the ion translocation site. Na+-binding converts the antiporter from the apo- or proton-bound, outward-open state to the Na+-bound, inward-open state. Oscillation between these two states result in rapid Na+/H+ antiport.

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Acta Cryst. (2010). A66, s18
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In this overview, we briefly outline recent advances in electron cryomicroscopy (cryoEM) and explain why the journal IUCrJ can provide a natural home for publications covering many present and future developments in the cryoEM field.


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Controlled devitrification of vitreous samples for high-resolution single-particle cryo-EM reduces beam-induced motion in the critical early frames of a movie stack by a factor of approximately four.

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Acta Cryst. (2014). A70, C1046
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Membrane proteins are essential to transport molecules across biological membranes. This gateway task makes them important drug targets. About 60% of all approved drugs target membrane proteins. Transport of ions across membranes is essential for every cell to maintain physiological salt concentrations and to keep pH homeostasis. In the past years X-Ray structures of various secondary transporters have provided insight into the mechanisms of membrane transport. However, difficulties in expression, purification and crystallization of membrane proteins still restrict the number of available structures. For well-characterized secondary transporters such as LeuT (1), BetP (2) and Ca2+/H+-exchangers (3) crystal structures in different conformations and substrate binding states have been obtained. However, for many important classes of transport proteins, detailed structures are urgently needed to understand their mechanism of action and to guide drug development. We report crystal structures of 2 homologues of a new secondary transporter in different states, with or without substrate bound. These structures shed light on the transport mechanism of this important class of membrane transport proteins.

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