title: Crystallization and preliminary X-ray diffraction analysis of FKBP52 N-terminal domain.
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%.
authors.affiliation: 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.
authors.forename: Pengyun
authors.initials: P
authors.lastname: Li
authors.forename: Cuiling
authors.initials: C
authors.lastname: Shu
authors.forename: Beili
authors.initials: B
authors.lastname: Wu
authors.forename: Yi
authors.initials: Y
authors.lastname: Ding
authors.forename: Beifen
authors.initials: B
authors.lastname: Shen
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D022021:Tacrolimus Binding Proteins / Q000737:chemistry*
chemical_list: D022021:Tacrolimus Binding Proteins; C403485:tacrolimus binding protein 4