Key result
A stable intramolecular complex comprising the LIM domains of Isl1 tethered to a peptide region of Ldb1 was engineered, purified, and crystallized, diffracting to 3.10 Å resolution.
The study successfully crystallized the Isl1-Ldb1 complex, diffracting to 3.10 Å resolution, enabling future structural analysis.
A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Isl1 tethered to a peptide region of Ldb1 has been engineered, purified and crystallized. The orthorhombic crystals belonged to space group P222(1), with unit-cell parameters a=57.2, b=56.7, c=179.8 Å, and diffracted to 3.10 Å resolution.
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Gadd et al. (2012) studied this question. Isl1-Ldb1 complex crystallization was evaluated on Crystallization and diffraction resolution. A stable intramolecular complex comprising the LIM domains of Isl1 tethered to a peptide region of Ldb1 was engineered, purified, and crystallized, diffracting to 3.10 Å resolution.
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