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Preliminary X-ray diffraction study of the wild-type and a mutationally-altered tryptophan synthetase α subunit

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

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Citation

Schulz, G. E., & Creighton, T. E. (1969). Preliminary X-ray diffraction study of the wild-type and a mutationally-altered tryptophan synthetase α subunit. The FEBS Journal, 10(2), 195-197. doi:10.1111/j.1432-1033.1969.tb00673.x.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-60E9-E
Abstract
Single crystals of the tryptophan synthetase α subunit of Escherichia coli suitable for X-ray diffraction analysis have been obtained. The diffraction pattern of a mutationally-altered α subunit (α-33) has been compared with that of the wild-type subunit. No significant differences in unit cell dimensions or in relative intensities of individual reflections at low diffraction angles were apparent. It is concluded that the mutational replacement of the glutamic acid residue at position 48 by methionine causes no more than a small alteration of the subunit's conformation, although the enzymatic activity of the subunit has been abolished.