Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood
- 1 December 1999
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 55 (12) , 2053-2055
- https://doi.org/10.1107/s0907444999012883
Abstract
The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5α-dihydrotestosterone (DHT) in two different crystal forms. Native data sets have been collected for tetragonal crystals (space group P4122 or P4322; unit-cell parameters a = 52.2, c = 148.4 Å) diffracting to 3.3 Å and trigonal crystals (R32; a = 104.0, c = 84.4 Å) diffracting to better than 1.6 Å. Since both crystal forms can only accommodate a single monomer in the asymmetric unit and share twofold rotational symmetry, it is proposed that the homodimer of this truncated form of SHBG, as observed in ultracentrifugation experiments, displays C 2 point-group symmetry.Keywords
This publication has 0 references indexed in Scilit: