title: Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization.
abstract: 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 P4(3)2(1)2, 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.
authors: Division of Molecular Structure, MRC - National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, England.
authors: Benjamin
authors: B
authors: Stieglitz
authors: Katrin
authors: K
authors: Rittinger
authors: Lesley F
authors: LF
authors: Haire
mesh_terms: D057205:Automation, Laboratory; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D014452:Ubiquitins / Q000737:chemistry*
chemical_list: D002352:Carrier Proteins; C575183:SHARPIN protein, human; D014452:Ubiquitins