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Crystallization and preliminary X-ray crystallographic study of the human MST2 SARAH domain.

ABSTRACT: The SARAH domain at the C-terminus of human MST2 (residues 436-484) was overproduced and purified using an Escherichia coli expression system. The purified domain was crystallized using the hanging-drop vapour-diffusion technique. Two crystal forms were obtained. The crystals belonged to space group P2, with unit-cell parameters a = 62.0, b = 119.2, c = 62.0 Å, ? = 90.0, ? = 90.5, ? = 90.0°, or to space group P6(1)22, with unit-cell parameters a = 54.5, b = 54.5, c = 303.1 Å. These crystals diffracted to 2.7 and 3.0 Å resolution, respectively.

SUBMITTER: Song J

PROVIDER: S-EPMC3212461 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic study of the human MST2 SARAH domain.

Song Jinsue J Hong Hyerim H Choi Saehae S Lee Yong Hee YH Yamashita Eiki E Bae Suk Chul SC Park Il Yeong IY Lee Soo Jae SJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20111027 Pt 11

The SARAH domain at the C-terminus of human MST2 (residues 436-484) was overproduced and purified using an Escherichia coli expression system. The purified domain was crystallized using the hanging-drop vapour-diffusion technique. Two crystal forms were obtained. The crystals belonged to space group P2, with unit-cell parameters a = 62.0, b = 119.2, c = 62.0 Å, α = 90.0, β = 90.5, γ = 90.0°, or to space group P6(1)22, with unit-cell parameters a = 54.5, b = 54.5, c = 303.1 Å. These crystals diff ...[more]

PMID: 22102242

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