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  • 标题:X-ray diffraction of rat tail tendon at ambient and cryo-cooled temperatures - a comparison
  • 本地全文:下载
  • 作者:J. H. Laing ; J.P.R.O. Orgel ; J. Dubochet
  • 期刊名称:Fibre Diffraction Review : the CCP13 Newsletter ; Software Development for Fibre Diffraction (Formerly The CCP13 Newsletter)
  • 印刷版ISSN:1463-8401
  • 电子版ISSN:1463-8401
  • 出版年度:2003
  • 卷号:11
  • 出版社:CCLRC Daresbury Laboratory
  • 摘要:Rat-tail tendon is primarily composed of type I collagen fibres in which the collagen molecules are axially packed according to the quarter-stagger model (Hodge and Petruska (1963). This arrangement produces the characteristic meridional series of reflections in the X-ray diffraction pattern of this tissue. Crystalline-like lateral packing interactions produce a series of discrete but often overlapping Bragg reflections arranged as rowlines in the equatorial plane of the X-ray diffraction pattern. Analysis of the equatorial reflections reveals that the collagen molecules are packed on a nonstandard quasi-hexagonal lattice, where the unit cell is triclinic (Fraser et al.,1983; 1987; Wess et al., 1995; 1998; Orgel et al., 2001). The equatorial rowlines are overlaid by a continuous layer of diffuse scatter, thought to arise from liquid-like molecular disorder, particularly in the gap region (Hulmes et al., 1995). Some of the diffuse scatter is removed on cryo-cooling the sample to 90-100 Kelvin during data collection and some non-physically by mathematical means (Wess et al., 1998). Analysis of the component underlying Bragg peaks and of the distribution and intensity of the diffuse scatter at different temperatures will help to further clarify the positions, mobilities and paths of the molecular segments within the gap and overlap regions of the triclinic unit cell.
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