Published November 17, 2016
| Version v1
Dataset
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Original X-ray diffraction images for 5-aminolevulinic acid dehydratase (ALAD) from E. coli complexed with porphobilinogen.
Authors/Creators
- 1. University of Southampton
- 2. UCL
Description
The diffraction images which allowed the original 2.1 Angstrom resolution structure determination of Escherichia coli ALAD co-crystallised with a non-covalently bound moiety of the product, porphobilinogen (PBG), are presented.
Notes
This dataset complements another dataset collected from a different crystal of the same complex: https://zenodo.org/record/51560
Files
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(186.8 MB)
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Additional details
Related works
- Is supplemented by
- 10.5281/zenodo.51560 (DOI)
References
- Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis. Mills-Davies, N., Butler, D., Norton, E., Thompson, D., Sarwar, M., Guo, J., Gill, R., Azim, N., Coker, A., Wood, S. P., Erskine, P. T., Coates, L., Cooper, J. B., Rashid, N., Akhtar, M and Shoolingin-Jordan, P. M. (2017). Acta Cryst. D73, 9-21.