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

Tengchuan Jin; Andrew J. Howard; Erica A. Golemis; Yingtong Wang; Yu Zhu Zhang

doi:10.1107/S1744309105002861

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

Tengchuan Jin, Andrew J. Howard, Erica A. Golemis, Yingtong Wang, Yu Zhu Zhang

Illinois Institute of Technology

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

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 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.

Original language	English
Pages (from-to)	282-284
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	3
DOIs	https://doi.org/10.1107/S1744309105002861
State	Published - 2005

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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 {\AA}, β = 92.484°, and diffract to at least 1.50 {\AA}. A SeMet derivative of the protein was prepared and crystallized for MAD phasing.",

author = "Tengchuan Jin and Howard, {Andrew J.} and Golemis, {Erica A.} and Yingtong Wang and Zhang, {Yu Zhu}",

year = "2005",

doi = "10.1107/S1744309105002861",

language = "English",

volume = "61",

pages = "282--284",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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publisher = "John Wiley and Sons Ltd",

number = "3",

}

Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B. / Jin, Tengchuan; Howard, Andrew J.; Golemis, Erica A. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 3, 2005, p. 282-284.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Overproduction, purification, crystallization and preliminary X-ray diffraction studies of the human spliceosomal protein TXNL4B

AU - Jin, Tengchuan

AU - Howard, Andrew J.

AU - Golemis, Erica A.

AU - Wang, Yingtong

AU - Zhang, Yu Zhu

PY - 2005

Y1 - 2005

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AB - 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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DO - 10.1107/S1744309105002861

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EP - 284

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 3

ER -

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

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