ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Purification, crystallization and preliminary X-ray analysis of human histidine decarboxylase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Identification of histidine decarboxylase and its multi-enzyme cascade system for cost-efficient biosynthesis of carcinine.3 Biotech · 2025Article
- Histamine, Metabolic Remodelling and Angiogenesis: A Systems Level Approach.Biomolecules · 2021Review
- Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase.The Journal of biological chemistry · 2012Article
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Authors and funding
4 authors.
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Abstract
The core domain of a human histidine decarboxylase mutant was purified and cocrystallized with the inhibitor L-histidine methyl ester. Using synchrotron radiation, a data set was collected from a single crystal at 100 K to 1.8 Å resolution. The crystal belonged to space group C2, with unit-cell parameters a = 215.16, b = 112.72, c = 171.39 Å, β = 110.3°. Molecular replacement was carried out using the structure of aromatic L-amino-acid decarboxylase as a search model. The crystal contained three dimers per asymmetric unit, with a Matthews coefficient (V(M)) of 3.01 Å(3) Da(-1) and an estimated solvent content of 59.1%.
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