r-axis rapid ii imaging plate diffractometer (Rigaku Corporation)
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r-axis rapid ii imaging plate diffractometer
R Axis Rapid Ii Imaging Plate Diffractometer, 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/r-axis+imaging+plate+system/xrd+patterns/pmc10582418__ADVS___10___2207440___s001-119-10-9
Average 90 stars, based on 1 article reviews
R Axis Rapid Ii Imaging Plate Diffractometer, 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/r-axis+imaging+plate+system/xrd+patterns/pmc10582418__ADVS___10___2207440___s001-119-10-9
Average 90 stars, based on 1 article reviews
r-axis rapid ii imaging plate diffractometer - by Bioz Stars,
2026-10
90/100 stars
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X-ray Diffraction:Article Title: Characterization of Crystalline Formate Dehydrogenase H from Escherichia coli Article Snippet: Preliminary Crystallographic Analysis of FDH Crystals—A typical Article Title: Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease. Article Snippet: nature structural biology • volume 5 number 9 • september 1998 819 1Boehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road / P.O.. Box 368, Ridgefield, Connecticut 06877, USA.. 2Boehringer Ingelheim (Canada) Ltd., Bio-Méga Research Division, 2100 rue Cunard, Laval, Québec, Canada H7S 2G5. Article Title: Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Article Snippet: The p38 MAP kinase plays a crucial role in regulating the production of proinflammatory cytokines, such as tumor necrosis factor and interleukin-1.. Blocking this kinase may offer an effective therapy for treating many inflammatory diseases.. Here we report a new allosteric binding site for a diaryl urea class of highly potent and selective inhibitors against human p38 MAP kinase. Article Title: Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution. Article Snippet: Department of Inflammatory src homology 2 (SH2) domains are modules of about 100 amino acid Diseases, Boehringer residues and bind to phosphotyrosine-containing motifs in a sequencespecific manner.. They play important roles in intracellular signal Ingelheim Pharmaceuticals transduction and represent potential targets for pharmacological intervenInc., 900 Ridgebury Road P.O.. Box 368, Ridgefield tion. Article Title: Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. Article Snippet: 0022±2836/97/160137±10 $25.00/0/mb The ef®cient and correct folding of bacterial disul®de bonded proteins in vivo is dependent upon a class of periplasmic oxidoreductase proteins called DsbA, after the Escherichia coli enzyme.. In the pathogenic bacterium Vibrio cholerae, the DsbA homolog (TcpG) is responsible for the folding, maturation and secretion of virulence factors.. Mutants in which the tcpg gene has been inactivated are avirulent; they no longer produce functional colonisation pili and they no longer secrete cholera toxin. Article Title: Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding. Article Snippet: X-ray diffraction data to 1.8 Å resolution were collected at cryotemperature on a R-Axis imaging plate system mounted on a Article Title: Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. Article Snippet: The structures of two ternary complexes of wheat serine carboxypeptidase Institute of Molecular Biology and Departments of II (CPD-WII), with a tetrapeptide aldehyde and a reaction product arginine, have been determined by X-ray crystallography at room temperature and Physics and Biology University of Oregon, Eugene −170°.. The peptide aldehydes, antipain and chymostatin, form covalent adducts with the active-site serine 146.. The CPD-WII antipain arginine OR 97403, USA model has a standard crystallographic R-factor of 0.162, with good Department of Chemistry geometry at 2.5 Å resolution for data collected at room temperature. Imaging:Article Title: Characterization of Crystalline Formate Dehydrogenase H from Escherichia coli Article Snippet: Preliminary Crystallographic Analysis of FDH Crystals—A typical Article Title: Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease. Article Snippet: nature structural biology • volume 5 number 9 • september 1998 819 1Boehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road / P.O.. Box 368, Ridgefield, Connecticut 06877, USA.. 2Boehringer Ingelheim (Canada) Ltd., Bio-Méga Research Division, 2100 rue Cunard, Laval, Québec, Canada H7S 2G5. Article Title: Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Article Snippet: The p38 MAP kinase plays a crucial role in regulating the production of proinflammatory cytokines, such as tumor necrosis factor and interleukin-1.. Blocking this kinase may offer an effective therapy for treating many inflammatory diseases.. Here we report a new allosteric binding site for a diaryl urea class of highly potent and selective inhibitors against human p38 MAP kinase. Article Title: Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution. Article Snippet: Department of Inflammatory src homology 2 (SH2) domains are modules of about 100 amino acid Diseases, Boehringer residues and bind to phosphotyrosine-containing motifs in a sequencespecific manner.. They play important roles in intracellular signal Ingelheim Pharmaceuticals transduction and represent potential targets for pharmacological intervenInc., 900 Ridgebury Road P.O.. Box 368, Ridgefield tion. Article Title: Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. Article Snippet: 0022±2836/97/160137±10 $25.00/0/mb The ef®cient and correct folding of bacterial disul®de bonded proteins in vivo is dependent upon a class of periplasmic oxidoreductase proteins called DsbA, after the Escherichia coli enzyme.. In the pathogenic bacterium Vibrio cholerae, the DsbA homolog (TcpG) is responsible for the folding, maturation and secretion of virulence factors.. Mutants in which the tcpg gene has been inactivated are avirulent; they no longer produce functional colonisation pili and they no longer secrete cholera toxin. Article Title: Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding. Article Snippet: X-ray diffraction data to 1.8 Å resolution were collected at cryotemperature on a R-Axis imaging plate system mounted on a Article Title: Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. Article Snippet: The structures of two ternary complexes of wheat serine carboxypeptidase Institute of Molecular Biology and Departments of II (CPD-WII), with a tetrapeptide aldehyde and a reaction product arginine, have been determined by X-ray crystallography at room temperature and Physics and Biology University of Oregon, Eugene −170°.. The peptide aldehydes, antipain and chymostatin, form covalent adducts with the active-site serine 146.. The CPD-WII antipain arginine OR 97403, USA model has a standard crystallographic R-factor of 0.162, with good Department of Chemistry geometry at 2.5 Å resolution for data collected at room temperature. Generated:Article Title: Characterization of Crystalline Formate Dehydrogenase H from Escherichia coli Article Snippet: Preliminary Crystallographic Analysis of FDH Crystals—A typical Article Title: Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease. Article Snippet: nature structural biology • volume 5 number 9 • september 1998 819 1Boehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road / P.O.. Box 368, Ridgefield, Connecticut 06877, USA.. 2Boehringer Ingelheim (Canada) Ltd., Bio-Méga Research Division, 2100 rue Cunard, Laval, Québec, Canada H7S 2G5. Article Title: Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Article Snippet: The p38 MAP kinase plays a crucial role in regulating the production of proinflammatory cytokines, such as tumor necrosis factor and interleukin-1.. Blocking this kinase may offer an effective therapy for treating many inflammatory diseases.. Here we report a new allosteric binding site for a diaryl urea class of highly potent and selective inhibitors against human p38 MAP kinase. Article Title: Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution. Article Snippet: Department of Inflammatory src homology 2 (SH2) domains are modules of about 100 amino acid Diseases, Boehringer residues and bind to phosphotyrosine-containing motifs in a sequencespecific manner.. They play important roles in intracellular signal Ingelheim Pharmaceuticals transduction and represent potential targets for pharmacological intervenInc., 900 Ridgebury Road P.O.. Box 368, Ridgefield tion. Article Title: Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. Article Snippet: 0022±2836/97/160137±10 $25.00/0/mb The ef®cient and correct folding of bacterial disul®de bonded proteins in vivo is dependent upon a class of periplasmic oxidoreductase proteins called DsbA, after the Escherichia coli enzyme.. In the pathogenic bacterium Vibrio cholerae, the DsbA homolog (TcpG) is responsible for the folding, maturation and secretion of virulence factors.. Mutants in which the tcpg gene has been inactivated are avirulent; they no longer produce functional colonisation pili and they no longer secrete cholera toxin. Article Title: Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding. Article Snippet: X-ray diffraction data to 1.8 Å resolution were collected at cryotemperature on a R-Axis imaging plate system mounted on a Article Title: Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. Article Snippet: The structures of two ternary complexes of wheat serine carboxypeptidase Institute of Molecular Biology and Departments of II (CPD-WII), with a tetrapeptide aldehyde and a reaction product arginine, have been determined by X-ray crystallography at room temperature and Physics and Biology University of Oregon, Eugene −170°.. The peptide aldehydes, antipain and chymostatin, form covalent adducts with the active-site serine 146.. The CPD-WII antipain arginine OR 97403, USA model has a standard crystallographic R-factor of 0.162, with good Department of Chemistry geometry at 2.5 Å resolution for data collected at room temperature. |