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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.

SUBMITTER: Stieglitz B

PROVIDER: S-EPMC3388930 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization.

Stieglitz Benjamin B Rittinger Katrin K Haire Lesley F LF

Acta crystallographica. Section F, Structural biology and crystallization communications 20120628 Pt 7

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 crystal ...[more]

PMID: 22750873

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