| Literature DB >> 22102242 |
Jinsue Song1, Hyerim Hong, Saehae Choi, Yong Hee Lee, Eiki Yamashita, Suk Chul Bae, Il Yeong Park, Soo Jae Lee.
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, 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 diffracted to 2.7 and 3.0 Å resolution, respectively.Entities:
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Year: 2011 PMID: 22102242 PMCID: PMC3212461 DOI: 10.1107/S1744309111033823
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091