x-stream cryogenic crystal cooler system msc (Rigaku Corporation)
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Rigaku Corporation
x-stream cryogenic crystal cooler system msc
X Stream Cryogenic Crystal Cooler System Msc, supplied by Rigaku Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/set+data+streaming+remote+operator/x+streamtm+2000+cryocooling+system/pm12454461-56-14-11
Average 90 stars, based on 1 article reviews
X Stream Cryogenic Crystal Cooler System Msc, supplied by Rigaku Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/set+data+streaming+remote+operator/x+streamtm+2000+cryocooling+system/pm12454461-56-14-11
Average 90 stars, based on 1 article reviews
x-stream cryogenic crystal cooler system msc - by Bioz Stars,
2026-10
90/100 stars
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Produced:Article Title: Anti-PHF-tau antibodies and uses thereof Article Snippet: The crystal was flash-cooled in liquid nitrogen, and data were collected on a Article Title: Structural insights into humanization of anti-tissue factor antibody 10H10 Article Snippet: The crystals were flash cooled in liquid nitrogen at 100 K. Diffraction data for the Fab were collected using a MicroMax-007HF microfocus X-ray generator equipped with an Osmic VariMax confocal optics, Saturn 944 CCD detector, and an Article Title: Structural Insight into the Mechanism of PALB2 Interaction with MRG15 Article Snippet: Diffraction was collected using the departmental X-ray facility with a Article Title: Interferon alpha and omega antibody antagonists Article Snippet: For X-ray data collection, one crystal of IFN-ω/Fab IFWM371 complex was soaked for a few seconds in the Article Title: Surface salt bridges contribute to the extreme thermal stability of an FN3-like domain from a thermophilic bacterium. Article Snippet: This study uses differential scanning calorimetry, X-ray crystallography and molecular dynamics simulations to investigate the structural basis for the high thermal stability (melting temperature 97.5 °C) of a FN3-like protein domain from thermophilic bacteria Thermoanaerobacter tengcongensis (FN3tt).. FN3tt adopts a typical FN3 fold with a three-stranded beta sheet packing against a four-stranded beta sheet.. We identified three solvent exposed arginine residues (R23, R25 and R72), which stabilize the protein through salt bridge interactions with glutamic acid residues on adjacent strands. Article Title: Structure-based peptide inhibitors of alpha-synuclein aggregation Article Snippet: The plate was agitated at 37° C., with a 3 mm rotation diameter, at 300 rpm in a Varioskan microplate reader (Thermo). Article Title: Structure-based peptide inhibitors of α-synuclein aggregation Article Snippet: Aligned fibrils or nanocrystals were mounted onto a cryopin for diffraction using 1.54 Å x-rays produced by a Article Title: Prodrug and protected forms of 5-hydroxymethylfurfuranal (5-HMF) and its derivatives Article Snippet: Cherry-red needle crystals formed in 1-3 days for Imaging:Article Title: Anti-PHF-tau antibodies and uses thereof Article Snippet: The crystal was flash-cooled in liquid nitrogen, and data were collected on a Article Title: Structural insights into humanization of anti-tissue factor antibody 10H10 Article Snippet: The crystals were flash cooled in liquid nitrogen at 100 K. Diffraction data for the Fab were collected using a MicroMax-007HF microfocus X-ray generator equipped with an Osmic VariMax confocal optics, Saturn 944 CCD detector, and an Article Title: Structural Insight into the Mechanism of PALB2 Interaction with MRG15 Article Snippet: Diffraction was collected using the departmental X-ray facility with a Article Title: Interferon alpha and omega antibody antagonists Article Snippet: For X-ray data collection, one crystal of IFN-ω/Fab IFWM371 complex was soaked for a few seconds in the Article Title: Surface salt bridges contribute to the extreme thermal stability of an FN3-like domain from a thermophilic bacterium. Article Snippet: This study uses differential scanning calorimetry, X-ray crystallography and molecular dynamics simulations to investigate the structural basis for the high thermal stability (melting temperature 97.5 °C) of a FN3-like protein domain from thermophilic bacteria Thermoanaerobacter tengcongensis (FN3tt).. FN3tt adopts a typical FN3 fold with a three-stranded beta sheet packing against a four-stranded beta sheet.. We identified three solvent exposed arginine residues (R23, R25 and R72), which stabilize the protein through salt bridge interactions with glutamic acid residues on adjacent strands. Article Title: Structure-based peptide inhibitors of alpha-synuclein aggregation Article Snippet: The plate was agitated at 37° C., with a 3 mm rotation diameter, at 300 rpm in a Varioskan microplate reader (Thermo). Article Title: Structure-based peptide inhibitors of α-synuclein aggregation Article Snippet: Aligned fibrils or nanocrystals were mounted onto a cryopin for diffraction using 1.54 Å x-rays produced by a Article Title: Prodrug and protected forms of 5-hydroxymethylfurfuranal (5-HMF) and its derivatives Article Snippet: Cherry-red needle crystals formed in 1-3 days for |