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Crystallization and diffraction of an Isl1-Ldb1 complex.


ABSTRACT: 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.

SUBMITTER: Gadd MS 

PROVIDER: S-EPMC3515390 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

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Crystallization and diffraction of an Isl1-Ldb1 complex.

Gadd Morgan S MS   Jacques David A DA   Guss J Mitchell JM   Matthews Jacqueline M JM  

Acta crystallographica. Section F, Structural biology and crystallization communications 20121030 Pt 11


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. ...[more]

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