Work

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

Year: 2005

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309105002861

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

Institutions: Illinois Institute of Technology, Fox Chase Cancer Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

OpenAlex ID: W2024478657

FWCI: 0.202

Cites: 13

Cited by: 3

Related to: 10