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EC Number	Crystallization (Commentary)	Reference
1.14.14.12	hanging drop vapor-diffusion method at 18°C, the crystal structure of HsaA to 2.5 A resolution reveales that the enzyme has the same fold, flavin-binding site, and catalytic residues as p-hydroxyphenyl acetate hydroxylase. HsaA prepared aerobically from the Escherichia coli host exists as a mixture of dimers and octamers in solution while HsaA prepared anaerobically from the rhodococcal host exists as a tetramer	715515

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Release 2023.1 (January 2023)