Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures

Autor:	Holger Stark, F. Zemlin, Christoph Boettcher
Rok vydání:	1996
Předmět:	Diffraction Spots biology Liquid helium Chemistry Analytical chemistry Bacteriorhodopsin Liquid nitrogen Atomic and Molecular Physics and Optics Electronic Optical and Magnetic Materials law.invention Coolant law Radiation damage biology.protein Protein crystallization Instrumentation
Zdroj:	Ultramicroscopy. 63:75-79
ISSN:	0304-3991
Popis:	A series of diffraction patterns from two-dimensional protein crystals of bacteriorhodopsin (purple membrane) at different temperatures (294 K, 98 K and 4 K) were recorded as the diffraction spots faded due to radiation damage. The patterns were then computationally evaluated in order to obtain a quantitative measurement of the structural preservation while irradiating the specimen. To provide statistically significant results, diffraction spots corresponding to spacings of 3A(1200 spots) and 7A(600 spots) were measured. A substantial increase of the lifetime of high resolution spots was found using liquid nitrogen as a coolant, whereas further structural preservation at liquid helium temperature was significant but smaller. It appears likely therefore that high resolution images are accessible even at liquid nitrogen temperature. Mechanical stability and the absence of thermal specimen drift are certainly of equivalent importance for successful high resolution imaging.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c2d606a6c354a2670599923e63537069 https://doi.org/10.1016/0304-3991(96)00045-9 Zobrazit plný text záznamu Full Text from ScienceDirect