Original X-Ray Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
Original X-Ray Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
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.
Protein crystallography, structural biology, tetrapyrrole biosynthesis
Norton, Edwin
00910b84-1247-475e-a413-65ff62127727
Shoolingin-Jordan, Peter
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Erskine, Peter
69c13bdf-c4a8-41e7-bbee-74f52f4b3095
Cooper, Jonathan
812eb501-58ac-4357-8fd7-21f7b947f512
Norton, Edwin
00910b84-1247-475e-a413-65ff62127727
Shoolingin-Jordan, Peter
ac0bf2cc-ee36-4b30-bcef-525cee2559f7
Erskine, Peter
69c13bdf-c4a8-41e7-bbee-74f52f4b3095
Cooper, Jonathan
812eb501-58ac-4357-8fd7-21f7b947f512
Norton, Edwin, Shoolingin-Jordan, Peter, Erskine, Peter and Cooper, Jonathan
(2016)
Original X-Ray Diffraction Images For 5-Aminolevulinic Acid Dehydratase (Alad) From E. Coli Complexed With Porphobilinogen.
Zenodo
doi:10.5281/zenodo.167137
[Dataset]
Abstract
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.
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Published date: 2016
Keywords:
Protein crystallography, structural biology, tetrapyrrole biosynthesis
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Local EPrints ID: 434465
URI: http://eprints.soton.ac.uk/id/eprint/434465
PURE UUID: dea5dc7d-4bf9-40b9-a4ee-d2d86e46f251
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Date deposited: 24 Sep 2019 16:31
Last modified: 26 Feb 2024 18:27
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Creator:
Edwin Norton
Creator:
Peter Erskine
Creator:
Jonathan Cooper
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