626 twin cold stage (Gatan Inc)
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Gatan Inc
626 twin cold stage
626 Twin Cold Stage, supplied by Gatan Inc, used in various techniques. Bioz Stars score: 99/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/626+twin+cold+stage/Alpine+Direct+Detection+Camera/pmc02253458-142-24-23
Average 99 stars, based on 99 article reviews
626 Twin Cold Stage, supplied by Gatan Inc, used in various techniques. Bioz Stars score: 99/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/626+twin+cold+stage/Alpine+Direct+Detection+Camera/pmc02253458-142-24-23
Average 99 stars, based on 99 article reviews
626 twin cold stage - by Bioz Stars,
2026-09
99/100 stars
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Microscopy:Article Title: Structural changes in GroEL effected by binding a denatured protein substrate. Article Snippet: 0022-2836/01/040569±9 $35.00/0 In the absence of nucleotides or cofactors, the Escherichia coli chaperonin GroEL binds select proteins in non-native conformations, such as denatured glutamine synthetase (GS) monomers, preventing their aggregation and spontaneous renaturation.. The nature of the GroEL-GS complexes thus formed, speci®cally the effect on the conformation of the GroEL tetradecamer, has been examined by electron microscopy.. We ®nd that specimens of GroEL-GS are visibly heterogeneous, due to incomplete loading of GroEL with GS. Article Title: Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase Article Snippet: .. Images of PhK were recorded at a magnification of 60,000 using minimal dose protocols with a JEOL 1200EX electron microscope equipped with a Article Title: Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase Article Snippet: .. Image analysis Images of PhK were recorded at a magnification of 60,000 using minimal dose protocols with a JEOL 1200EX electron microscope equipped with a Cryo-Electron Microscopy:Article Title: Structural changes in GroEL effected by binding a denatured protein substrate. Article Snippet: 0022-2836/01/040569±9 $35.00/0 In the absence of nucleotides or cofactors, the Escherichia coli chaperonin GroEL binds select proteins in non-native conformations, such as denatured glutamine synthetase (GS) monomers, preventing their aggregation and spontaneous renaturation.. The nature of the GroEL-GS complexes thus formed, speci®cally the effect on the conformation of the GroEL tetradecamer, has been examined by electron microscopy.. We ®nd that specimens of GroEL-GS are visibly heterogeneous, due to incomplete loading of GroEL with GS. |