Crystallization and preliminary X-ray crystallographic analysis of yeast prion protein Ure2p with shortened N-terminal |
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Authors: | Liwei Wang Li Zhu Junmei Zhou Zihe Rao |
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Institution: | WANG Liwei, ZHU Li, ZHOU Junmei & RAO Zihe 1. Laboratory of Structural Biology, Department of Biological Sciences and Biotechnology & Protein Sciences Laboratory of MOE, Tsinghua University, Beijing 100084, China; 2. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China |
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Abstract: | An orthorhombic crystal form of a recombinant yeast prion protein with shortened N-terminal, 90Ure2p, has been obtained. Crystals were grown by the vapordiffusion technique against a mother liquor containing imidazole. Crystals belong to the primitive orthorhombic lattice with the cell parameters a = 54.5 Å, b = 74.7 Å, c = 131.0 Å. The crystals diffract to beyond 3.0 Å resolution at a synchrotron beamline. |
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Keywords: | yeast prion Ure2p crystallization |
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