Determination of the structure of selenomethionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion

Hädener, A.; Matzinger, P.K.; Battersby, A.R.; McSweeney, S.; Thompson, A.W.; Hammersley, A.P.; Harrop, S.J.; Cassetta, A.; Deacon, A.; Hunter, W.N.; Nieh, Y.P.; Raftery, J.; Hunter, N.; Helliwell, J.R.

doi:10.1107/S0907444998014711

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 1
The biosynthesis of uroporphyrinogen III from 5-aminolevulinic acid. The enzymes involved are (a) 5-aminolaevulinic acid dehydratase; (b) hydroxymethylbilane synthase (HMBS); and (c) uroporphyrinogen III synthase. A = CH₂COO⁻; P = CH₂CH₂COO⁻.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 55| Part 3| March 1999| Pages 631-643

doi:10.1107/S0907444998014711

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page