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EC Number Crystallization (Commentary)
Show all pathways known for 4.1.2.19Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.19-
Show all pathways known for 4.1.2.19Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.19hanging drop method, crystallizes in space group P3(2)21
Show all pathways known for 4.1.2.19Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.19mutant enzymes by hanging drop vapour diffusion method, with 100 mM sodium acetate pH 4.5, 50% (v/v) ethylene glycol and 5% (w/v) PEG1000
Show all pathways known for 4.1.2.19Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.19structure established at 1.35 A resolution in a crystal form that is obtained by a surface mutation and has one subunit of the C4-symmetric tetramer in the asymmetric unit. Crystals of the wild-type enzyme with their 20 crystallographically asymmetric subunits diffract to only 2.7 A resolution are much too complex for a convenient analysis of structural modifications. For both reasons, a more suitable crystal form is obtained by producing the six point mutants W8T, Q51R, Q52E, D98Y, E192A and E254R at the protein surface far away from the active center
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