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Journal Article

Crystals of partially trypsin-digested elongation factor Tu

MPS-Authors
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Gast,  Wolfgang H.
Max Planck Institute for Medical Research, Max Planck Society;

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Gast,  Wolfgang H.
Max Planck Institute for Medical Research, Max Planck Society;

Leberman,  Reuben
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schulz,  Georg E.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/0022283676903442/pdf?md5=fe845dfd1a4193d2feaa93198a8c3e0c&pid=1-s2.0-0022283676903442-main.pdf
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Citation

Gast, W. H., Gast, W. H., Leberman, R., Schulz, G. E., & Wittinghofer, A. (1976). Crystals of partially trypsin-digested elongation factor Tu. Journal of Molecular Biology (London), 106(4), 943-950. doi:10.1016/0022-2836(76)90344-2.


Cite as: https://hdl.handle.net/21.11116/0000-0002-AC7B-3
Abstract
Limited tryptic digestion of elongation factor Tu from Escherichia coli and Bacillus stearothermophilus at room temperature produces a small number of scissions without concomitant loss of GDP binding activity. The small number of large tryptic fragments produced are not separated by gel filtration under non-denaturing conditions and they coelute with the GDP binding activity. Crystals of the trypsin-treated elongation factor Tu from E. coli obtained from polyethylene glycol solutions are apparently identical to the pseudotetragonal crystals previously reported (Sneden et al., 1973).