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Figure 5
(a) Optimization of the crystallization pH using bis-Tris propane buffer. (b) Optimization of the protein concentration. (c) Crystal structure of the GBA dimer obtained at 1.56 Å resolution (PDB entry 6tjk). N-Glycans are depicted in glycoblock format (McNicholas & Agirre, 2017BB2). (d) GBA monomer comprising of three domains: domain I (residues 1–27 and 383–414) is shown in blue, domain II (residues 30–75 and 431–497) in red and domain III (residues 76–381 and 416–430) in gold. The active site contains bound bis-Tris propane, which forms hydrogen bonds to Trp179, Asn234, Glu235, Glu340, Trp381 and an ethylene glycol (EDO) cryoprotectant molecule. Electron density is contoured to 1σ (0.34 e Å−3). (e) Overlay of recombinant GBA (gold) obtained at pH 7.0 and Cerezyme (teal) obtained at pH 4.6 (PDB entry 6tjj).

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