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Purification, crystallization and preliminary X‐ray diffraction studies of the β‐catenin homolog HMP‐2 from Caenorhabditis elegans
Author(s) -
Choi HeeJung,
Weis William I.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000643
Subject(s) - caenorhabditis elegans , wnt signaling pathway , crystallization , crystallography , cell adhesion , catenin , biology , cell , chemistry , signal transduction , microbiology and biotechnology , biochemistry , gene , organic chemistry
β‐Catenin is a multifunctional protein involved in both cell adhesion and Wnt signaling in metazoans. The nematode Caenorhabditis elegans is unusual in that it expresses four β‐catenin paralogs with separate functions. C. elegans HMP‐2 participates in cell adhesion but not in Wnt signaling, so structural and biochemical studies of this protein will help in understanding its unusual specialization and the evolution of β‐catenin. HMP‐2 was expressed, purified and crystallized in two different salt conditions. Crystals grown from a sodium formate condition diffracted to a resolution of 2 Å and belonged to space group C 2, with unit‐cell parameters a = 165.2, b = 39.0, c = 101.1 Å, β = 116.7°. Crystals obtained from a lithium sulfate condition diffracted to 3 Å resolution and belonged to space group P 4 3 , with unit‐cell parameters a = b = 85.3, c = 138.7 Å. Diffraction data were collected and processed from both crystal forms and the structure was solved by molecular replacement. Model refinement is in progress.