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Crystallization and preliminary X-ray diffraction analysis of FKBP52 N-terminal domain.

作者信息

Li Pengyun, Shu Cuiling, Wu Beili, Ding Yi, Shen Beifen, Rao Zihe

机构信息

MOE Laboratory of Protein Science and Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2168-9. doi: 10.1107/s0907444902016396. Epub 2002 Nov 23.

Abstract

FKBP52 is a FK506-binding protein which was first discovered in the heterocomplex composed of HSP90 and inactive steroid receptor. Here, the N-terminal domain (residues 1-140) of FKBP52 has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion technique. Crystals with a 2.4 A resolution limit were obtained using ammonium sulfate as precipitant at pH 8.5. The crystals belong to space group P2(1), with unit-cell parameters a = 27.8, b = 58.4, c = 70.9 A, beta = 98.3 degrees. Assuming two molecules per asymmetric unit, the solvent content is calculated to be 40%.

摘要

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