Article info Vol. 5  No. 2   pp.  78 ~ 81
Title Purification, crystallization and X-ray crystallographic analysis of meso-diaminopimelic acid decarboxylase from Corynebacterium glutamicum
Authors Hyeoncheol Francis Son and Kyung-Jin Kim*
Institutions School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 41566, Korea. *Correspondence: kkim@knu.ac.kr
Abstract meso-Diaminopimelic acid decarboxylase from Corynebacterium glutamicum (CgDAPDC) is the key enzyme for the production of L -lysine and it catalyzes meso-DAP to produce the final product, L -lysine. The CgDAPDC was overexpressed and purified to homogeneity by Ni-NTA affinity and size-exclusion chromatography. The CgDAPDC protein was crystallized using sitting-drop vapor-diffusion method in the presence of 0.8 M sodium citrate tribasic and 0.1 M sodium cacodylate, pH 6.5 at 293 K. X-ray diffraction data were collected to a maximum resolution of 2.4 Å. The crystal belonged to space group P2 1 2 1 2, with unit cell parameters a = 114.54 Å, b = 91.702 Å, c = 95.161, α = β = γ = 90°. With one molecules per asymmetric unit, the crystal volume per unit protein mass was 2.64 Å 3 Da -1 , which correspond to a solvent content of approximately 53.37%.