An N-terminal fragment of human SHARPIN was recombinantly expressed in Escherichia coli, purified and crystallized. Crystals suitable for X-ray diffraction were obtained by a one-step optimization of seed dilution and protein concentration using a two-dimensional grid screen. The crystals belonged to the primitive tetragonal space group P43212, with unit-cell parameters a = b = 61.55, c = 222.81 Å. Complete data sets were collected from native and selenomethionine-substituted protein crystals at 100 K to 2.6 and 2.0 Å resolution, respectively. © 2012 International Union of Crystallography All rights reserved.
Stieglitz, B., Rittinger, K., & Haire, L. F. (2012). Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(7), 816–819. https://doi.org/10.1107/S1744309112022208