Abstract
The PSD-95 (postsynaptic density-95) protein, one of the members of the MAGUK (membrane-associated guanylate kinase) family, is composed of three PDZ domains, one SH3 domain and one guanylate kinase-like (GK) domain. The GK domain mediates the scaffolding function of PSD-95 by protein--protein interaction. Here, the GK domain was subcloned, expressed as an intein fusion protein, purified without the intein and then crystallized at room temperature by the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant. The complete native data set was collected to a resolution of 2.35 A using flash-cooling. The crystals belong to the primitive tetragonal space group P4(3) (or P4(1)), with unit-cell parameters a = b = 70.03 (4), c = 37.64 (1) A.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Chromatography, Affinity
-
Crystallization
-
Disks Large Homolog 4 Protein
-
Guanylate Kinases
-
Intracellular Signaling Peptides and Proteins
-
Membrane Proteins
-
Nerve Tissue Proteins / chemistry*
-
Nerve Tissue Proteins / isolation & purification
-
Nucleoside-Phosphate Kinase / chemistry*
-
Protein Structure, Tertiary
-
Rats
-
Recombinant Fusion Proteins / chemistry
-
Recombinant Fusion Proteins / isolation & purification
-
Substrate Specificity
-
X-Ray Diffraction
Substances
-
Disks Large Homolog 4 Protein
-
Dlg4 protein, rat
-
Intracellular Signaling Peptides and Proteins
-
Membrane Proteins
-
Mpp2 protein, rat
-
Nerve Tissue Proteins
-
Recombinant Fusion Proteins
-
postsynaptic density proteins
-
Nucleoside-Phosphate Kinase
-
Guanylate Kinases