Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2

In this study, the C-terminal SCP-2 domain of human HSDL2, including residues Lys318–Arg416, was produced in Escherichia coli, purified and crystallized. X-ray diffraction data were collected to 2.10 Å resolution. The crystal belonged to the trigonal space group P3121 (or P3221), with unit-cell parameters a = b = 70.4, c = 60.6 Å, α = β = 90, γ = 120°. Two protein molecules are present in the asymmetric unit, resulting in a Matthews coefficient of 2.16 Å3 Da−1 and an approximate solvent content of 43%.

Source: Acta Crystallographica Section F - June 27, 2015 Category: Biochemistry Authors: Cheng, Z.Li, Y.Sui, C.Sun, X.Xie, Y. Tags: human HSDL2 SCP-2 domian crystallization X-ray diffraction research communications Source Type: research