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Volumn 18, Issue 5, 2008, Pages 601-608

Experimental approaches for solution X-ray scattering and fiber diffraction

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID;

EID: 53249132537     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.08.002     Document Type: Review
Times cited : (27)

References (48)
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    • Evolution of long-range myofibrillar crystallinity in insect flight muscle as examined by X-ray cryomicrodiffraction
    • A technically impressive paper that required ground-breaking work in techniques of cryo-preservation, sample manipulation and micro-beam diffraction to obtain 'end-on' diffraction patterns from a range of insect muscles.
    • Iwamoto H., Inoue K., and Yagi N. Evolution of long-range myofibrillar crystallinity in insect flight muscle as examined by X-ray cryomicrodiffraction. Proc Biol Sci 273 (2006) 677-685. A technically impressive paper that required ground-breaking work in techniques of cryo-preservation, sample manipulation and micro-beam diffraction to obtain 'end-on' diffraction patterns from a range of insect muscles.
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    • Microfibrillar structure of type I collagen in situ
    • The authors used multiple isomorphous replacements to solve crystallographically the supermolecular packing structure of collagen type I in its natural fibrous form at a level where the molecular conformation of each collagen segment is defined in the very large unit cell. This structure paves the way to a molecular understanding of the action of collagen binding proteins such as decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
    • Orgel J.P., Irving T.C., Miller A., and Wess T.J. Microfibrillar structure of type I collagen in situ. Proc Natl Acad Sci U S A 103 (2006) 9001-9005. The authors used multiple isomorphous replacements to solve crystallographically the supermolecular packing structure of collagen type I in its natural fibrous form at a level where the molecular conformation of each collagen segment is defined in the very large unit cell. This structure paves the way to a molecular understanding of the action of collagen binding proteins such as decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9001-9005
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    • Cooperative deformation of mineral and collagen in bone at the nanoscale
    • This paper is an excellent example of how X-ray diffraction on third generation sources can be used to provide a structural explanation for the physical properties of a complex biological material, in this case, bone. We can expect that the study of naturally occurring and synthetic biomaterials will become even more important in future.
    • Gupta H.S., Seto J., Wagermaier W., Zaslansky P., Boesecke P., and Fratzl P. Cooperative deformation of mineral and collagen in bone at the nanoscale. Proc Natl Acad Sci U S A 103 (2006) 17741-17746. This paper is an excellent example of how X-ray diffraction on third generation sources can be used to provide a structural explanation for the physical properties of a complex biological material, in this case, bone. We can expect that the study of naturally occurring and synthetic biomaterials will become even more important in future.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17741-17746
    • Gupta, H.S.1    Seto, J.2    Wagermaier, W.3    Zaslansky, P.4    Boesecke, P.5    Fratzl, P.6
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    • Collagen organization in the chicken cornea and structural alterations in the retinopathy, globe enlarged (rge) phenotype--an X-ray diffraction study
    • Boote C., Hayes S., Jones S., Quantock A.J., Hocking P.M., Inglehearn C.F., Ali M., and Meek K.M. Collagen organization in the chicken cornea and structural alterations in the retinopathy, globe enlarged (rge) phenotype--an X-ray diffraction study. J Struct Biol 161 (2008) 1-8
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    • Boote, C.1    Hayes, S.2    Jones, S.3    Quantock, A.J.4    Hocking, P.M.5    Inglehearn, C.F.6    Ali, M.7    Meek, K.M.8
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    • Diffraction to study protein and peptide assemblies
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    • Helix-turn-helix peptides that form alpha-helical fibrils: turn sequences drive fibril structure
    • This paper shows that a very short amino acid sequence in a strategic part of the peptide could induce the fibrilogenesis of α-helical-based fibers including a previously not observed 'cross-α' fibril structure, that is, fibrilogenesis is not exclusively due to cross-β structures as is widely assumed.
    • Lazar K.L., Miller-Auer H., Getz G.S., Orgel J.P., and Meredith S.C. Helix-turn-helix peptides that form alpha-helical fibrils: turn sequences drive fibril structure. Biochemistry 44 (2005) 12681-12689. This paper shows that a very short amino acid sequence in a strategic part of the peptide could induce the fibrilogenesis of α-helical-based fibers including a previously not observed 'cross-α' fibril structure, that is, fibrilogenesis is not exclusively due to cross-β structures as is widely assumed.
    • (2005) Biochemistry , vol.44 , pp. 12681-12689
    • Lazar, K.L.1    Miller-Auer, H.2    Getz, G.S.3    Orgel, J.P.4    Meredith, S.C.5
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    • X-Ray fiber and powder diffraction of PrP prion peptides
    • This comprehensive review provides a good overview of prion biology and how diffraction techniques have contributed to our knowledge of prion structure.
    • Inouye H., and Kirschner D.A. X-Ray fiber and powder diffraction of PrP prion peptides. Adv Protein Chem 73 (2006) 181-215. This comprehensive review provides a good overview of prion biology and how diffraction techniques have contributed to our knowledge of prion structure.
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    • Inouye, H.1    Kirschner, D.A.2
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    • A microbeam X-ray diffraction study of insulin spherulites
    • This paper provides an excellent demonstration of the utility of microbeam diffraction to obtain structural information from complex biological structures.
    • Yagi N., Ohta N., Iida T., and Inoue K. A microbeam X-ray diffraction study of insulin spherulites. J Mol Biol 362 (2006) 327-333. This paper provides an excellent demonstration of the utility of microbeam diffraction to obtain structural information from complex biological structures.
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    • Yagi, N.1    Ohta, N.2    Iida, T.3    Inoue, K.4
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    • Dose, exposure time and resolution in serial X-ray crystallography
    • This paper makes the technical case for using a stream of oriented macromolecules in a high intensity, coherent X-ray beam from either specialized beamlines on third generation sources or upcoming fourth generation sources.
    • Starodub D., Rez P., Hembree G., Howells M., Shapiro D., Chapman H.N., Fromme P., Schmidt K., Weierstall U., Doak R.B., et al. Dose, exposure time and resolution in serial X-ray crystallography. J Synchrotron Radiat 15 (2008) 62-73. This paper makes the technical case for using a stream of oriented macromolecules in a high intensity, coherent X-ray beam from either specialized beamlines on third generation sources or upcoming fourth generation sources.
    • (2008) J Synchrotron Radiat , vol.15 , pp. 62-73
    • Starodub, D.1    Rez, P.2    Hembree, G.3    Howells, M.4    Shapiro, D.5    Chapman, H.N.6    Fromme, P.7    Schmidt, K.8    Weierstall, U.9    Doak, R.B.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.