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