Cloning, expression, purification, crystallization and initial crystallographic analysis of transcription elongation factors GreB from Escherichia coli and Gfh1 from Thermus thermophilus

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Anna A PerederinaDmitry G Vassylyev

Abstract

The Escherichia coli gene encoding the transcription cleavage factor GreB and the Thermus thermophilus gene encoding the anti-GreA transcription factor Gfh1 were cloned and expressed and the purified proteins were crystallized by the sitting-drop vapor-diffusion technique. The GreB and Gfh1 crystals, which were improved by macroseeding, belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 148, c = 115.2 A and a = b = 59.3, c = 218.9 A, respectively. Complete diffraction data sets were collected for the GreB and Gfh1 crystals to 2.6 and 2.8 A resolution, respectively. Crystals of the selenomethionine proteins were obtained by microseeding using the native protein crystals and diffract as well as the native ones. The structure determination of these proteins is now in progress.

References

Oct 19, 2001·The Journal of Biological Chemistry·Brian P HoganDorothy A Erie
Sep 6, 2002·Biochimica Et Biophysica Acta·Rachel N Fish, Caroline M Kane
Dec 12, 2003·Proceedings of the National Academy of Sciences of the United States of America·Ekaterina SosunovaArkady Mustaev
Jan 10, 2004·Methods in Enzymology·Oleg Laptenko, Sergei Borukhov
Apr 28, 2004·Cell·Irina ArtsimovitchDmitry G Vassylyev
Apr 6, 2005·Molecular Cell·Maria L KireevaMikhail Kashlev

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Citations

Jul 29, 2015·Proceedings of the National Academy of Sciences of the United States of America·Eric J Strobel, Jeffrey W Roberts
Sep 10, 2019·Nucleic Acids Research·Ranjit K PrajapatiGeorgiy A Belogurov
Apr 3, 2020·Proceedings of the National Academy of Sciences of the United States of America·Flint Stevenson-JonesNikolay Zenkin

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