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EC Number	Crystallization (Commentary)
2.1.1.189	crystal structures of apo-form RlmCD and its complex with SAH. A long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity
2.1.1.189	purified recombinant His-tagged enzyme, microbatch-under-oil technique by mixing 0.002 ml of each of protein and buffer solution (1:1 ratio) at 4°C and 20°C, initial crystal hits of the protein PhRlmCD are obtained in three different buffer conditions: (1) 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 1.0 M lithium sulfate monohydrate, (2) 0.1 M Bis-Tris, pH 5.5, and 2.0 M ammonium sulfate, (3) 0.1 M HEPES sodium, pH 7.5, 2% v/v PEG 400, and 2.0 M ammonium sulfate, at 20°C, crystal structure analysis at 3.2 A resolution, PDB ID 8Z62, overview
2.1.1.189	structure of RlmCD in complex with its cofactor and the RNA substrate containing U747 at 2.00 A or U1939 at 3.10 A. The side-chain rearrangement of F145 displays an unusual mechanism through which RlmCD can discriminate between U747- and U1939-containing RNA substrate by switching the intermolecular aromatic stacking between protein and RNA on/off
2.1.1.189	structure to 3.2 A resolution in the space group P212121 with two protomers in each asymmetric unit

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Release 2026.1 (March 2026)