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

• 발행기관: 한국구조생물학회
• 저자명: Jihye Seok Kyung-Jin Kim
• 간행물 정보: 『Biodesign』Vol 8, No 3, Sep, 68~71쪽, 전체 4쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2020.09.30

영문 초록

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%.

목차

INTRODUCTION

MATERIALS AND METHODS

RESULTS AND DISCUSSION

CONFLICT OF INTEREST

ACKNOWLEDGEMENTS

REFERENCES