The Experts below are selected from a list of 36 Experts worldwide ranked by ideXlab platform
Kohki Ishikawa - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X‐ray analysis of brazzein, a new sweet Protein
Acta Crystallographica Section D Biological Crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F. AbilgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
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Crystallization and preliminary X-ray analysis of brazzein, a new sweet Protein.
Acta crystallographica. Section D Biological crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F AbildgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
Armando J. Parodi - One of the best experts on this subject based on the ideXlab platform.
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Protein Sweetener
Nature, 2002Co-Authors: Armando J. ParodiAbstract:After years of failure, a Protein involved in flipping certain oligosaccharide molecules into the endoplasmic reticulum — one of the cellular sites where Proteins are modified with sugars — has been tracked down.
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Cell biology: Protein Sweetener
Nature, 2002Co-Authors: Armando J. ParodiAbstract:After years of failure, a Protein involved in flipping certain oligosaccharide molecules into the endoplasmic reticulum — one of the cellular sites where Proteins are modified with sugars — has been tracked down.
F Abildgaad - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X-ray analysis of brazzein, a new sweet Protein.
Acta crystallographica. Section D Biological crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F AbildgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
F. Abilgaad - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X‐ray analysis of brazzein, a new sweet Protein
Acta Crystallographica Section D Biological Crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F. AbilgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
H. Sasaki - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X‐ray analysis of brazzein, a new sweet Protein
Acta Crystallographica Section D Biological Crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F. AbilgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
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Crystallization and preliminary X-ray analysis of brazzein, a new sweet Protein.
Acta crystallographica. Section D Biological crystallography, 1996Co-Authors: Kohki Ishikawa, Masaru Tanokura, M. Ota, Y. Ariyoshi, H. Sasaki, D. Ming, J. Caldwell, F AbildgaadAbstract:Brazzein is a sweet Protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble Protein Sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.
