Bulk preparation and crystallization of the Escherichia coli elongation factor Tu-Ts complex

Yoder, Marilyn D.; Tores, Clare; Corelli, Robin L.; Jurnak, Frances

doi:10.1016/0003-2697(85)90466-x

Cited by 7 publications

(2 citation statements)

References 19 publications

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“…More information concerning the EF-Tu:EF-Ts interaction could come from Xray analysis of EF-Ts and the EF-Tu: EF-Ts complex. Though crystals of this complex have been obtained [23][24] no structure has been reported. In this work we report a possible two-domain-structure of EF-Ts and the successful crystallization and preliminary X-ray investigation of a 25 kDa C-terminal fragment obtained by tryptic digestion of cloned and overexpressed intact EF-Ts from E. coll.…”

Section: Introductionmentioning

confidence: 99%

Analysis and crystallization of a 25 kDa C‐terminal fragment of cloned elongation factor Ts fromEscherichia coli

et al. 1995

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A 25 kDa C-terminal tryptic fragment of elongation factor "Is has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exchange activity. Crystals of the C-terminal fragment belong to space group P2 or P21. The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours.

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Section: Introductionmentioning

confidence: 99%

Analysis and crystallization of a 25 kDa C‐terminal fragment of cloned elongation factor Ts fromEscherichia coli

et al. 1995

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“…The second form diffracted to better than 3.0A and was observed sporadically. Improvement in EF-Tu-Ts complex purity (Yoder, Torres, Corelli & Jurnak, 1985) and extensive crystallization screens of ion type and concentration failed to influence the poor reproducibility of the high-resolution crystal form. Because both crystal forms were sensitive to radiation damage, with half lives of 2 h or less at 293 K, effort was refocused on increasing the crystal stability by low-temperature data-collection methods (Hope, 1990;Petsko, 1975).…”

Section: Introductionmentioning

confidence: 99%

Extension of the diffraction resolution of crystals

Schick

Jurnak²

1994

Acta Cryst D

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The diffraction resolution of crystals of the guanine nucleotide-exchange factor complex, EF-Tu-Ts, has been extended from 5.0 to 2.5 A by lowering the solvent content in the crystals as well as the temperature of data collection. The common form of EF-Tu-Ts crystal belongs to space group P212121 with a = 81.1, b = 109.9, c = 207.5 A and has a solvent content of 61%. The crystals diffract to a resolution of 5.0 A, at 293 K and 4.0 A at 273 K. When cryoprotective agents are slowly diffused into the crystals, the cell constants slu'ink to a = 74.4, b = 109.9, c = 198.7A and the solvent content falls to 55%.

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Preparation of Escherichia coli elongation factor tu-guanosine 5′-triphosphate analogs

Delaria

Jurnak

1989

Analytical Biochemistry

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Bulk preparation and crystallization of the Escherichia coli elongation factor Tu-Ts complex

Cited by 7 publications

References 19 publications

Analysis and crystallization of a 25 kDa C‐terminal fragment of cloned elongation factor Ts fromEscherichia coli

Analysis and crystallization of a 25 kDa C‐terminal fragment of cloned elongation factor Ts fromEscherichia coli

Extension of the diffraction resolution of crystals

Preparation of Escherichia coli elongation factor tu-guanosine 5′-triphosphate analogs

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