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Protein Crystallography using Synchrotron Radiation. An Application of Multiwavelength Anomalous Diffraction Method.
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- NAKAGAWA Atsushi
- 高エネルギー物理学研究所放射光実験施設
Bibliographic Information
- Other Title
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- 放射光利用によるタンパク質の結晶構造解析 多波長異常分散法の利用
- ホウシャコウ リヨウ ニ ヨル タンパクシツ ノ ケッショウ コウゾウ カイセ
- —An Application of Multiwavelength Anomalous Diffraction Method—
- ―多波長異常分散法の利用―
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Description
Synchrotron radiation (SR) is an extremely useful X-ray source for protein crystallography. It is high brilliance, high intensity and small divergence white X-ray source, which enables us to collect high resolution diffraction data of biological macromolecular crystals with large cell dimensions. Furthermore, wavelength tunability of SR is essential for the phase determination by multiwavelength anomalous diffraction (MAD) method, which has a possibility of the direct phase determination of metal proteins, selenomethionyl proteins and proteins with single isomorphous derivative of poor isomorphism.<BR>MAD method is applied for the structure determination of cytochrome c-553 from Desulfovibrio vulgaris Miyazaki F strain.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 36 (6), 345-355, 1994
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679062973056
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- NII Article ID
- 130000788073
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 3595194
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed