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 A, beta = 92.484 degrees,, and diffract to at least 1.50 A. A SeMet derivative of the protein was prepared and crystallized for MAD phasing.
Jin
Tengchuan
T
Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
Howard
Andrew J
AJ
Golemis
Erica A
EA
Wang
Yingtong
Y
Zhang
Yu-Zhu
YZ
D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000737:chemistry; D006801:Humans; D009687:Nuclear Proteins; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D015183:Restriction Mapping; D017381:Spliceosomes / Q000737:chemistry*; D013879:Thioredoxins / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D018797:Cell Cycle Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; C506013:TXNL4B protein, human; D013879:Thioredoxins