pISSN 2288-6982
eISSN 2288-7105




BioDesign 2020; 8(3): 68-71

Published online September 30, 2020

© Korean Society for Structural Biology

Purification, crystallization and X-ray crystallographic analysis of glycine oxidase from Bacillus cereus ATCC 14579

Jihye Seok and Kyung-Jin Kim*

School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu 41566, Republic of Korea

Correspondence to:

Received: August 16, 2020; Revised: August 28, 2020; Accepted: August 31, 2020


Glycine oxidase (GO) is an enzyme that catalyzes the oxidation reaction of the primary and secondary amine of glycine. In this study, we overexpressed GO from Bacillus cereus ATCC 14579 (BcGO) and purified the protein to homogeneity by Ni-NTA affinity and size-exclusion chromatography. The BcGO protein was crystallized using hanging-drop vapordiffusion method in the presence of 15% (v/v) Tacsimate pH 7.0, 0.1 M HEPES pH 6.5, 6% (w/v) PEG 3350 at 293 K. X-ray diffraction data were collected to a maximum resolution of 2.36 Å. The BcGO crystals belong to the space group C2221 with unit cell parameters a = 82.18 Å, b = 132.81 Å, c = 165.212 Å, α = 90 °, β = 90 °, γ = 90 °. With two molecules of BcGO per asymmetric unit, the crystal volume per unit of protein mass is 2.74 Å3 Da–1, which correspond to a solvent content is approximately 55.82%.