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Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B

Journal Article · · Acta Crystallographica. Section F
;  [1];  [2]; ;  [1]
  1. Department of Biology, Illinois Institute of Technology, Chicago, IL 60616 (United States)
  2. Fox Chase Cancer Center, Philadelphia, PA 19111 (United States)
Human spliceosomal protein TXNL4B was purified and crystallized. 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.
OSTI ID:
22355989
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 3 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English