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Titlebook: Crystallographic Methods and Protocols; Christopher Jones,Barbara Mulloy,Mark R. Sanderson Book 1996 Humana Press 1996

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發(fā)表于 2025-3-21 20:07:46 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Crystallographic Methods and Protocols
編輯Christopher Jones,Barbara Mulloy,Mark R. Sanderson
視頻videohttp://file.papertrans.cn/241/240665/240665.mp4
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Crystallographic Methods and Protocols;  Christopher Jones,Barbara Mulloy,Mark R. Sanderson Book 1996 Humana Press 1996
描述The volumes in the series, Methods in Molecular Biology, are conceived with the biochemist and molecular biologist in mind. The present book, Crystallographic Methods andProtocols, concentrates on the use of X-ray crystallography to solve the detailed three- dimensional structuresofproteins, nucleic acids, andtheir complexes. Such a structure determination is a major undertaking, demands expertise in a range of skills, and requires considerable resources. The biologically trained worker will probably first become involved when identifying an important scientific problem whose solution would benefit from a full structure. The protein or nucleic acid at issue must be sequenced and prepared to high purity in appropriate quantities, probably by either chemical synthesis for nucleic acids or genetic engineering for proteins. CrystallographicMethods andPro- tocols aims to give biologically trained workers an insight into the techniques used to crystallize their proteins, obtain the raw X-ray data, and solve and refine the structure. The aim ofa crystal structure determination is to provide infor- mation that will solve biologically relevant problems; that process normally requires a high
出版日期Book 1996
版次1
doihttps://doi.org/10.1385/0896032590
isbn_ebook978-1-59259-543-3Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 1996
The information of publication is updating

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Overexpression, Isolation, and Crystallization of Proteins,ructural analysis by X-ray crystallography. High-level gene expression has facilitated the purification of many proteins that are normally only expressed at low concentrations, as well as those that have proven difficult to purify to homogeneity from natural sources. Furthermore, advances in oligonu
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Preliminary Characterization of Crystals,ded to answer many important questions about the crystals. Do they diffract X-rays? Do they diffract to a suitable resolution? Are they stable in the X-ray beam? What is their overall symmetry? What are the dimensions of their repeating unit? How many protein molecules are in that repeating unit? Th
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Structure Determination Using Isomorphous Replacement,udes and the calculation of phases for each diffraction point (maximum). Although amplitudes can be directly measured from diffracting crystals, phases are indirectly determined, because there are no lenses that can bend and focus X-rays. Thus, methods were developed to calculate phases from the int
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Density Modification in X-Ray Crystallography,es measured experimentally and phases obtained with the multiple isomorphous replacement method. This method has poor precision, generating errors in the phases and therefore in the map. If the quality of the map is not sufficient to trace clearly a molecular model, it is necessary to improve the ph
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Refinement of Protein and Nucleic Acid Structures, and data collection; second, phase determination and calculation of electron density maps; and third, model building and refinement. This final part is necessary because the structural models arrived at after the first two steps are approximate and usually contain errors in the tracing of the macro
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Recent Developments for Crystallographic Refinement of Macromolecules,ea detectors, and data analysis by high performance computers and new computational techniques. In addition, recombinant gene technology in many cases allows the expression of large amounts of protein. This has resulted in an unprecedented increase in the number of protein crystal structures elucida
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