Henderson limit

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The Henderson limit is the absorbed dose from X-rays , which halves the intensity of the diffraction pattern in a cooled protein crystal . The term goes back to the work of Richard Henderson .

properties

The Henderson limit is around 2 × 10 7  Gy and plays a role in crystal structure analyzes as it is a measure of how much data can be obtained for a given radiation intensity. Due to the ionizing X-rays, the photoelectric effect triggers various reactions in the protein molecules, e.g. For example, radicals are formed , which in turn can lead to oxidation of methionines , reduction of cystines , crosslinking and decarboxylation of aspartic and glutamic acids . The limit can be increased by nanofilm crystallization.

literature

  • Claudio Nicolini: Nanobiotechnology and Nanobiosciences. (= Pan Stanford Series on Nanobiotechnology. Volume 1). Pan Stanford Publishing, 2009, ISBN 9789814241380 .
  • T. Petrova, VY Lunin, S. Ginell, A. Mitschler, Y. Kim, G. Joachimiak, A. Cousido-Siah, I. Hazemann, A. Podjarny, K. Lazarski, A. Joachimiak: X-ray Induced Cooperative Atomic Movement in a Protein Crystal . In: Randy Read, Alexandre G. Urzhumtsev, Vladimir Y. Lunin (Eds.): Advancing Methods for Biomolecular Crystallography . Springer, Dordrecht 2013, ISBN 978-94-007-6231-2 , chap. 9 , p. 91-104 .
  • EF Garman, M. Weik: Radiation Damage in Macromolecular Crystallography . In: Gwyndaf Evans, Konstantinos Beis (Ed.): Protein Crystallography: Challenges and Practical Solutions . Royal Society of Chemistry, Cambridge 2018, ISBN 978-1-78262-728-9 , chap. 4 , p. 88-116 .

Individual evidence

  1. ↑ Richard Henderson: Cryo-Protection of Protein Crystals against Radiation Damage in Electron and X-Ray Diffraction. In: Proc. R. Soc. Lond. B. Vol. 241, No. 1300, 1990, pp. 6-8, doi : 10.1098 / rspb . 1990.0057 .
  2. ↑ TY Teng, K. Moffat: Primary radiation damage of protein crystals by an intense synchrotron X-ray beam. In: Journal of synchrotron radiation. Volume 7, Pt. 5, 2000, ISSN  0909-0495 , pp. 313-317, doi : 10.1107 / S0909049500008694 , PMID 16609214 .
  3. ↑ E. Pechkova, C. Nicolini: protein nanocrystallography: a new approach to structural proteomics. In: Trends in biotechnology. Volume 22, number 3, 2004, ISSN  0167-7799 , pp. 117-122, doi : 10.1016 / j.tibtech.2004.01.011 , PMID 15036861 .