Hémonnot, Clément Y. J.

[["dc.bibliographiccitation.firstpage","3313"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biomacromolecules"],["dc.bibliographiccitation.lastpage","3321"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Hémonnot, Clément Y. J."],["dc.contributor.author","Mauermann, Monika"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","The intermediate filament proteins keratin K8 and K18 constitute an essential part of the cytoskeleton in simple epithelial cell layers, structurally enforcing their mechanical resistance. K8/K18 heterodimers form extended filaments and higher-order structures including bundles and networks that bind to cell junctions. We study the assembly of these proteins in the presence of monovalent or divalent ions by small-angle X-ray scattering. We find that both ion species cause an increase of the filament diameter when their concentration is increased; albeit, much higher values are needed for the monovalent compared to the divalent ions for the same effect. Bundling occurs also for monovalent ions and at comparatively low concentrations of divalent ions, very different from vimentin intermediate filaments, a fibroblast-specific cytoskeleton component. We explain these differences by variations in charge and hydrophobicity patterns of the proteins. These differences may reflect the respective physiological situation in stationary cell layers versus single migrating fibroblasts."],["dc.identifier.doi","10.1021/acs.biomac.5b00965"],["dc.identifier.gro","3141817"],["dc.identifier.isi","000362863500025"],["dc.identifier.pmid","26327161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1401"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1526-4602"],["dc.relation.issn","1525-7797"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Assembly of Simple Epithelial Keratin Filaments: Deciphering the Ion Dependence in Filament Organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1220"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","1223"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Saldanha, Oliva"],["dc.contributor.author","Graceffa, Rita"],["dc.contributor.author","Hémonnot, Clément Y. J."],["dc.contributor.author","Ranke, Christiane"],["dc.contributor.author","Brehm, Gerrit"],["dc.contributor.author","Liebi, Marianne"],["dc.contributor.author","Marmiroli, Benedetta"],["dc.contributor.author","Weihausen, Britta"],["dc.contributor.author","Burghammer, Manfred"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2018-02-12T12:27:30Z"],["dc.date.available","2018-02-12T12:27:30Z"],["dc.date.issued","2017"],["dc.description.abstract","Encapsulating reacting biological or chemical samples in microfluidic droplets has the great advantage over single‐phase flows of providing separate reaction compartments. These compartments can be filled in a combinatoric way and prevent the sample from adsorbing to the channel walls. In recent years, small‐angle X‐ray scattering (SAXS) in combination with microfluidics has evolved as a nanoscale method of such systems. Here, we approach two major challenges associated with combining droplet microfluidics and SAXS. First, we present a simple, versatile, and reliable device, which is both suitable for stable droplet formation and compatible with in situ X‐ray measurements. Second, we solve the problem of “diluting” the sample signal by the signal from the oil separating the emulsion droplets by multiple fast acquisitions per droplet and data thresholding. We show that using our method, even the weakly scattering protein vimentin provides high signal‐to‐noise ratio data."],["dc.identifier.doi","10.1002/cphc.201700221"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12175"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Rapid Acquisition of X-Ray Scattering Data from Droplet-Encapsulated Protein Systems"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3553"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","ACS Nano"],["dc.bibliographiccitation.lastpage","3561"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Hemonnot, Clement Y. J."],["dc.contributor.author","Reinhardt, Juliane"],["dc.contributor.author","Saldanha, Oliva"],["dc.contributor.author","Patommel, Jens"],["dc.contributor.author","Graceffa, Rita"],["dc.contributor.author","Weinhausen, Britta"],["dc.contributor.author","Burghammer, Manfred"],["dc.contributor.author","Schroer, Christian G."],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:54:36Z"],["dc.date.available","2017-09-07T11:54:36Z"],["dc.date.issued","2016"],["dc.description.abstract","In recent years, X-ray imaging of biological cells has emerged as a complementary alternative to fluorescence and electron microscopy. Different techniques were established and successfully applied to macromolecular assemblies and structures in cells. However, while the resolution is reaching the nanometer scale, the dose is increasing. It is essential to develop strategies to overcome or reduce radiation damage. Here we approach this intrinsic problem by combing two different X-ray techniques, namely ptychography and nanodiffraction, in one experiment and on the same sample. We acquire low dose ptychography overview images of whole cells at a resolution of 65 nm. We subsequently record high-resolution nanodiffraction data from regions of interest. By comparing images from the two modalities, we can exclude strong effects of radiation damage on the specimen. From the diffraction data we retrieve quantitative structural information from intracellular bundles of keratin intermediate filaments such as a filament radius of 5 nm, hexagonal geometric arrangement with an interfilament distance of 14 nm and bundle diameters on the order of 70 nm. Thus, we present an appealing combined approach to answer a broad range of questions in soft matter physics, biophysics and biology."],["dc.identifier.doi","10.1021/acsnano.5b07871"],["dc.identifier.gro","3141720"],["dc.identifier.isi","000372855400058"],["dc.identifier.pmid","26905642"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/324"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1936-086X"],["dc.relation.issn","1936-0851"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","X-rays Reveal the Internal Structure of Keratin Bundles in Whole Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]