The use of construct variation and diffraction data analysis in the crystallization of the TRAF domain of human tumor necrosis factor receptor associated factor 6.
Obtaining soluble proteins and diffraction-quality crystals often represents the bottleneck in macromolecular crystallography. Here, it is shown that construct variation can be an efficient strategy in expressing soluble proteins from bacteria and that clues from poor crystals may be used to improve crystal packing and to optimize crystal quality.
D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D008958:Models, Molecular; D020033:Protein Isoforms / Q000737:chemistry / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D018124:Receptors, Tumor Necrosis Factor / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012995:Solubility; D048029:TNF Receptor-Associated Factor 6
D020033:Protein Isoforms; D011506:Proteins; D018124:Receptors, Tumor Necrosis Factor; D011994:Recombinant Proteins; D048029:TNF Receptor-Associated Factor 6