Triple-axis x-ray diffraction analyses of hen egg-white lysozyme crystals
Autor: | H M Volz, R J Matyi |
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Rok vydání: | 2001 |
Předmět: |
Diffraction
Acoustics and Ultrasonics Chemistry Analytical chemistry Crystal structure Condensed Matter Physics Surfaces Coatings and Films Electronic Optical and Magnetic Materials Intensity (physics) Crystallography Tetragonal crystal system X-ray crystallography Angular resolution Irradiation Protein crystallization |
Zdroj: | Journal of Physics D: Applied Physics. 34:A64-A69 |
ISSN: | 1361-6463 0022-3727 |
DOI: | 10.1088/0022-3727/34/10a/314 |
Popis: | We have used high-resolution triple-axis x-ray diffraction analyses to monitor the defect structure in tetragonal crystals of hen egg-white lysozyme as a function of x-ray irradiation time. At long irradiation times we observed the expected decrease in peak intensity and increase in the angular extent of the peak breadth. In contrast, the initial stages of irradiation showed relatively complex changes in both the peak breadth and the intensity; in fact, during the period from 25 to 45 h of irradiation the angular breadth of the intensity (both the full-width at half-maximum and the full-width at 1% of the maximum intensity) decreased to a minimum value. We have found that the unambiguous analysis of defects at high angular resolution is complicated by the fact that the diffraction characteristics of protein crystals apparently lie at the confluence of the kinematic (ideally imperfect) and dynamic (ideally perfect) treatments of diffraction. |
Databáze: | OpenAIRE |
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