Purification,characterization, and crystallization of the adhesive domain of SdrD from Staphylococcus aureus |
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| Authors: | Liqing Zhang Hua Xiang Jinlan Gao Jia Hu Shiying Miao Linfang Wang Xuming Deng Shentao Li |
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| Institution: | 1. Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Changchun 130062, PR China;2. Liaoning Province Academy of Analytic Science, Shenyang 110015, PR China;3. College of Quartermaster Technology, Jilin University, Changchun 130062, PR China;1. Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, College of Veterinary Medicine, Jilin University, Xi''an Road 5333#, Changchun 130062, China;2. Laboratory Animal Center, Jilin University, Changchun 130062, Jilin, China;1. College of Veterinary Medicine, Jilin University, Changchun 130062, PR China;2. College of Animal Science and Technology, Jilin Agricultural University, Changchun 130118, PR China;3. Teaching Center of Basic Courses, Jilin University, Changchun 130062, PR China;4. Liaoning Province Academy of Analytic Science, Shenyang 110015, PR China;5. College of Animal Sciences, Jilin University, Changchun 130062, PR China |
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| Abstract: | The adhesive domain of SdrD from Staphylococcus aureus was solubly expressed in Escherichia coli in high yield. After a series of purification steps, the purified protein was >95% pure, which was SdrD from S. aureus identified by SDS–PAGE and MALDI-TOF MS. Crystals were grown at 18 °C using 25% polyethylene glycol 3350 as precipitant. Diffraction by the crystal extends to 1.65 Å resolution, and the crystal belongs to the space group C2, with the unit cell parameters a = 133.3, b = 58.3, c = 112.3 Å, α = 90.00, β = 111.14, γ = 90.00. |
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