Overproduction, purification, crystallization and preliminary X‐ray diffraction studies of the human spliceosomal protein TXNL4B
The human gene coding for the spliceosomal protein thioredoxin‐like 4B (TXNL4B) was overexpressed in Escherichia coli and the encoded protein was purified and crystallized. Well diffracting single crystals were obtained by the vapor‐diffusion method in hanging drops. The crystals belong to the primitive monoclinic space group P2, with unit‐cell parameters a = 39.0, b = 63.6, c = 51.0 Å, β = 92.484°, and diffract to at least 1.50 Å. A SeMet derivative of the protein was prepared and crystallized for MAD phasing.
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