Comparison of protein crystal diffraction patterns and absolute intensities 
from synchrotron and conventional X-ray sources

Harmsen , A.; Leberman, Reuben; Schulz, G. E.

doi:10.1016/0022-2836(76)90017-6

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Comparison of protein crystal diffraction patterns and absolute intensities from synchrotron and conventional X-ray sources

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Leberman, Reuben
Max Planck Institute for Medical Research, Max Planck Society;

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Schulz, G. E.
Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0022283676900176/pdf?md5=ffbcaf70ff7eb11118bbe7738ad00f7b&pid=1-s2.0-0022283676900176-main.pdf
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Citation

Harmsen, A., Leberman, R., & Schulz, G. E. (1976). Comparison of protein crystal diffraction patterns and absolute intensities from synchrotron and conventional X-ray sources. Journal of Molecular Biology (London), 104(1), 311-314. doi:10.1016/0022-2836(76)90017-6.

Cite as: https://hdl.handle.net/21.11116/0000-0002-ACA1-6

Abstract

X-ray diffraction photographs from crystals with cell dimensions between 50 Å and 250 Å have been obtained with synchrotron and conventional X-ray sources and compared qualitatively. For quantitative comparison the absolute intensities of the primary beams have been determined.