Analysis of collagen fibril diameter distribution in connective tissues using small-angle x-ray scattering.

K. L. Goh, J. Hiller, L. Haston, D. F. Holmes, K. E. Kadler, Ann Hird Murdoch, Judith Rowena Meakin, T. J. Wess

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Analysis of the diameters of collagen fibrils provides insight into the structure and physical processes occurring in the tissue. This paper describes a method for analyzing the frequency distribution of the diameters of collagen fibrils from small-angle X-ray scattering (SAXS) patterns. Frequency values of fibril diameters were input into a mathematical model of the form factor to calculate the equatorial intensity which best fits the experimentally derived data from SAXS patterns. A minimization algorithm utilizing simulated annealing (SA) was used in the fitting procedure. The SA algorithm allowed for random sampling of the frequency values, and was run iteratively to build up an optimized frequency distribution of fibril diameters. Results were obtained for collagen samples from sheep spine ligaments. The mean fibril diameter value obtained from this data-fitting method was 73 nm +/- 20 nm (S.D.). From scanning transmission electron microscopy, the mean diameter was found to be 69 nm +/- 14 nm (S.D.). The good agreement between the two methods demonstrates the reliability of the SAXS method for the tissue examined. The non-destructive nature of this technique, as well as its statistical robusticity and capacity for large sampling, means that this method is both quick and effective. (c) 2004 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)183-188
Number of pages5
JournalBiochimica et Biophysica Acta (BBA) - General Subjects
Volume1722
Issue number2
DOIs
Publication statusPublished - 2005

Keywords

  • collagen fibril diameter
  • scanning transmission electron microscopy
  • small-angle X-ray scattering
  • simulated annealing
  • TENDON
  • SIZE
  • MODEL
  • AGE
  • ARRANGEMENT
  • MORPHOLOGY
  • EXERCISE

Cite this

Analysis of collagen fibril diameter distribution in connective tissues using small-angle x-ray scattering. / Goh, K. L.; Hiller, J.; Haston, L.; Holmes, D. F.; Kadler, K. E.; Murdoch, Ann Hird; Meakin, Judith Rowena; Wess, T. J.

In: Biochimica et Biophysica Acta (BBA) - General Subjects, Vol. 1722, No. 2, 2005, p. 183-188.

Research output: Contribution to journalArticle

Goh, K. L. ; Hiller, J. ; Haston, L. ; Holmes, D. F. ; Kadler, K. E. ; Murdoch, Ann Hird ; Meakin, Judith Rowena ; Wess, T. J. / Analysis of collagen fibril diameter distribution in connective tissues using small-angle x-ray scattering. In: Biochimica et Biophysica Acta (BBA) - General Subjects. 2005 ; Vol. 1722, No. 2. pp. 183-188.
@article{64410243a26d491ea708b93c1249fcdf,
title = "Analysis of collagen fibril diameter distribution in connective tissues using small-angle x-ray scattering.",
abstract = "Analysis of the diameters of collagen fibrils provides insight into the structure and physical processes occurring in the tissue. This paper describes a method for analyzing the frequency distribution of the diameters of collagen fibrils from small-angle X-ray scattering (SAXS) patterns. Frequency values of fibril diameters were input into a mathematical model of the form factor to calculate the equatorial intensity which best fits the experimentally derived data from SAXS patterns. A minimization algorithm utilizing simulated annealing (SA) was used in the fitting procedure. The SA algorithm allowed for random sampling of the frequency values, and was run iteratively to build up an optimized frequency distribution of fibril diameters. Results were obtained for collagen samples from sheep spine ligaments. The mean fibril diameter value obtained from this data-fitting method was 73 nm +/- 20 nm (S.D.). From scanning transmission electron microscopy, the mean diameter was found to be 69 nm +/- 14 nm (S.D.). The good agreement between the two methods demonstrates the reliability of the SAXS method for the tissue examined. The non-destructive nature of this technique, as well as its statistical robusticity and capacity for large sampling, means that this method is both quick and effective. (c) 2004 Elsevier B.V. All rights reserved.",
keywords = "collagen fibril diameter, scanning transmission electron microscopy, small-angle X-ray scattering, simulated annealing, TENDON, SIZE, MODEL, AGE, ARRANGEMENT, MORPHOLOGY, EXERCISE",
author = "Goh, {K. L.} and J. Hiller and L. Haston and Holmes, {D. F.} and Kadler, {K. E.} and Murdoch, {Ann Hird} and Meakin, {Judith Rowena} and Wess, {T. J.}",
year = "2005",
doi = "10.1016/j.bbagen.2004.12.004",
language = "English",
volume = "1722",
pages = "183--188",
journal = "Biochimica et Biophysica Acta (BBA) - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Analysis of collagen fibril diameter distribution in connective tissues using small-angle x-ray scattering.

AU - Goh, K. L.

AU - Hiller, J.

AU - Haston, L.

AU - Holmes, D. F.

AU - Kadler, K. E.

AU - Murdoch, Ann Hird

AU - Meakin, Judith Rowena

AU - Wess, T. J.

PY - 2005

Y1 - 2005

N2 - Analysis of the diameters of collagen fibrils provides insight into the structure and physical processes occurring in the tissue. This paper describes a method for analyzing the frequency distribution of the diameters of collagen fibrils from small-angle X-ray scattering (SAXS) patterns. Frequency values of fibril diameters were input into a mathematical model of the form factor to calculate the equatorial intensity which best fits the experimentally derived data from SAXS patterns. A minimization algorithm utilizing simulated annealing (SA) was used in the fitting procedure. The SA algorithm allowed for random sampling of the frequency values, and was run iteratively to build up an optimized frequency distribution of fibril diameters. Results were obtained for collagen samples from sheep spine ligaments. The mean fibril diameter value obtained from this data-fitting method was 73 nm +/- 20 nm (S.D.). From scanning transmission electron microscopy, the mean diameter was found to be 69 nm +/- 14 nm (S.D.). The good agreement between the two methods demonstrates the reliability of the SAXS method for the tissue examined. The non-destructive nature of this technique, as well as its statistical robusticity and capacity for large sampling, means that this method is both quick and effective. (c) 2004 Elsevier B.V. All rights reserved.

AB - Analysis of the diameters of collagen fibrils provides insight into the structure and physical processes occurring in the tissue. This paper describes a method for analyzing the frequency distribution of the diameters of collagen fibrils from small-angle X-ray scattering (SAXS) patterns. Frequency values of fibril diameters were input into a mathematical model of the form factor to calculate the equatorial intensity which best fits the experimentally derived data from SAXS patterns. A minimization algorithm utilizing simulated annealing (SA) was used in the fitting procedure. The SA algorithm allowed for random sampling of the frequency values, and was run iteratively to build up an optimized frequency distribution of fibril diameters. Results were obtained for collagen samples from sheep spine ligaments. The mean fibril diameter value obtained from this data-fitting method was 73 nm +/- 20 nm (S.D.). From scanning transmission electron microscopy, the mean diameter was found to be 69 nm +/- 14 nm (S.D.). The good agreement between the two methods demonstrates the reliability of the SAXS method for the tissue examined. The non-destructive nature of this technique, as well as its statistical robusticity and capacity for large sampling, means that this method is both quick and effective. (c) 2004 Elsevier B.V. All rights reserved.

KW - collagen fibril diameter

KW - scanning transmission electron microscopy

KW - small-angle X-ray scattering

KW - simulated annealing

KW - TENDON

KW - SIZE

KW - MODEL

KW - AGE

KW - ARRANGEMENT

KW - MORPHOLOGY

KW - EXERCISE

U2 - 10.1016/j.bbagen.2004.12.004

DO - 10.1016/j.bbagen.2004.12.004

M3 - Article

VL - 1722

SP - 183

EP - 188

JO - Biochimica et Biophysica Acta (BBA) - General Subjects

JF - Biochimica et Biophysica Acta (BBA) - General Subjects

SN - 0304-4165

IS - 2

ER -