title: Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B.
abstract: 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.
authors.affiliation: Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
authors.forename: Tengchuan
authors.initials: T
authors.lastname: Jin
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Howard
authors.forename: Erica A
authors.initials: EA
authors.lastname: Golemis
authors.forename: Yingtong
authors.initials: Y
authors.lastname: Wang
authors.forename: Yu-Zhu
authors.initials: YZ
authors.lastname: Zhang
mesh_terms: 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
chemical_list: D018797:Cell Cycle Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; C506013:TXNL4B protein, human; D013879:Thioredoxins