Mass: 29164.166 Da / Num. of mol.: 1 / Fragment: L27 domain, L27 1/2 domain Source method: isolated from a genetically manipulated source Details: Structural Basis for Assembling a Tripartite Complex Dlg1-MPP7-Mals3 Source: (gene. exp.) Homo sapiens (human) / Gene: L27 domains of Dlg1, MPP7 and Mals3 Plasmid details: in-house-modified version of the pET32a vector (Novagen), in which the S-tag an d the thrombin recognition site were replaced by a sequence encoding a TEV prote ase cleavage site ...Plasmid details: in-house-modified version of the pET32a vector (Novagen), in which the S-tag an d the thrombin recognition site were replaced by a sequence encoding a TEV prote ase cleavage site (Glu-Asn-Leu-Tyr-Phe-Gln-Ser) Plasmid: pET32a vector (Novagen) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q12959, UniProt: Q5T2T1, UniProt: Q9NUP9
Mass: 18.015 Da / Num. of mol.: 41 / Source method: isolated from a natural source / Formula: H2O
Compound details
THE L27 DOMAINS OF HUMAN DLG1 (TERMED AS L27HDLG1), HUMAN MPP7 (TERMED AS L27N AND L27C) AND HUMAN ...THE L27 DOMAINS OF HUMAN DLG1 (TERMED AS L27HDLG1), HUMAN MPP7 (TERMED AS L27N AND L27C) AND HUMAN MALS3 (TERMED AS L27HMALS3) WERE COVALENTLY LINKED TOGETHER BY PRECISSION PROTEASE CLEAVAGE SITE AS ONE SINGLE POLYPEPTIDE.
Sequence details
THE INTERNAL SEQUENCE LEVLFQGP ARE LINKER.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 2
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Sample preparation
Crystal
Density Matthews: 3.42 Å3/Da / Density % sol: 64.04 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 10% PEG 8000, 0.2M MgCl2, 0.1M Guanidine HCl, 0.1M Tris-HCl, pH7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
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