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EC Number	Crystallization (Commentary)	Reference
2.7.1.39	crystal structure of the enzyme with ADP reveals a novel nucleotide binding fold. The N-terminal domain contains an unusual left-handed beta,alpha,beta unit, while the C-terminal domain has a central alpha-beta plait fold with an insertion of four helices	641474
2.7.1.39	crystals are grown by the hanging drop vapor diffusion method	641474, 641475
2.7.1.39	purified recombinant His-tagged enzyme in apoform or with either methionine or ATPgammaS and cysteine, hanging drop vapor diffusion method, mixing of 0.002 ml of 16.2 mg/ml protein in 20 mM Tris, pH 7.5, 150 mM NaCl, 50 mM KCl, and 50 mM MgCl2 with 0.002 ml of well solution containing 0.25 M ammonium sulfate, 25% PEG 3350, and 0.1 M HEPES, pH 7.5, and equilibration against 0.1 ml of well solution, X-ray diffraction structure determination and analysis at 1.8-2.2 A resolution	758579
2.7.1.39	the enzyme ternary complexes with its amino acid substrate and ATP analogues determined by X-ray crystallography	641475

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Release 2023.1 (January 2023)