Work

Purification, crystallization and preliminary X-ray analysis of human histidine decarboxylase

Year: 2012

Type: article

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%.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309112015692

Authors: Hirofumi Komori, Yoko Nitta, Hiroshi Ueno, Yoshiki Higuchi

Institutions: University of Hyogo, SPring-8, RIKEN, Nara Women's University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Kawanishi Memorial ShinMaywa Education Foundation, Academia Sinica, Japan Society for the Promotion of Science

Awards: Development of the eating-habits assessment for patients with the end stage diabetic renal disease, Development of comprehensive nutrition support system for the elderly people with psychiatric disorder, Relationship between oral allergy syndrome and bio active amine in saliva, Structural Study of the Mechanism of Hydrogen Activation on Ni-enzymes, Reaction Mechansim of [NiFe]-hydrogenase by Neutron Structural Chmeistry