Author:
Lu Qianda,Ma Jinming,Rong Hui,Fan Jun,Yuan Ye,Li Kuai,Gao Yongxiang,Zhang Xiao,Teng Maikun,Niu Liwen
Abstract
5-Aminolaevulinic acid dehydratase (ALAD), a crucial enzyme in the biosynthesis of tetrapyrrole, catalyses the condensation of two 5-aminolaevulinic acid (ALA) molecules to form porphobilinogen (PBG). The gene encoding ALAD was amplified from genomic DNA ofBacillus subtilisand the protein was overexpressed inEscherichia colistrain BL21 (DE3). The protein was purified and crystallized with an additional MGSSHHHHHHSSGLVPRGSH– tag at the N-terminus of the target protein. Diffraction-quality single crystals were obtained by the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected at a resolution of 2.7 Å.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
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