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Crystallization and diffraction of an Lhx4-Isl2 complex.

ABSTRACT: A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P2(1), with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 A, beta = 111.9 degrees, and diffracted to 2.16 A resolution.

SUBMITTER: Gadd MS

PROVIDER: S-EPMC2635870 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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Crystallization and diffraction of an Lhx4-Isl2 complex.

Gadd Morgan S MS Langley David B DB Guss J Mitchell JM Matthews Jacqueline M JM

Acta crystallographica. Section F, Structural biology and crystallization communications 20090131 Pt 2

A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P2(1), with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 A, beta = 111.9 degrees, and diffracted to 2.16 A resolution. ...[more]

PMID: 19194008

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