Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes.

Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes.
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DOI:
10.1016/s1570-9639(02)00460-0
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发表时间:
2002-12
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
H. Karring;G. Andersen;S. Thirup;J. Nyborg;L. Spremulli;B. Clark
H. Karring;G. Andersen;S. Thirup;J. Nyborg;L. Spremulli;B. Clark
中科院分区:
其他
文献类型:
--
作者:
H. Karring;G. Andersen;S. Thirup;J. Nyborg;L. Spremulli;B. Clark

文献摘要

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Previous studies have shown that when bovine mitochondrial elongation factor Ts (EF-Ts) is expressed in Escherichia coli, it forms a tightly associated complex with E. coli elongation factor Tu (EF-Tu). In contrast to earlier experiments, purification of free mitochondrial EF-Ts was accomplished under nondenaturing conditions since only about 60% of the expressed EF-Ts copurified with E. coli EF-Tu. The bovine mitochondrial EF-Tu:GDP complex, the homologous mitochondrial EF-Tu:EF-Ts complex, and the heterologous E. coli/mitochondrial EF-Tu:EF-Ts complex were isolated and crystallised. The crystals of the EF-Tu:GDP complex diffract to 1.94 Å and belong to space group P21with cell parameters a=59.09 Å, b=119.78 Å, c=128.89 Å and β=96.978°. The crystals of the homologous mitochondrial EF-Tu:EF-Ts complex diffract to 4 Å and belong to space group C2 with cell parameters a=157.7 Å, b=151.9 Å, c=156.9 Å, and β=108.96°.