Literature summary for 6.3.4.22 extracted from

Osawa, T.; Inanaga, H.; Kimura, S.; Terasaka, N.; Suzuki, T.; Numata, T.
Crystallization and preliminary X-ray diffraction analysis of an archaeal tRNA-modification enzyme, TiaS, complexed with tRNA(Ile2) and ATP (2011), Acta Crystallogr. Sect. F, 67, 1414-1416.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escherichia coli	Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment)	Organism
the enzyme is cocrystallized with both tRNAIle2 and ATP by the vapour-diffusion method. The crystals of the TiaStRNAIle2ATP complex diffract to 2.9 A resolution. The crystals belong to the hexagonal space group P3(2)21, with unit-cell parameters a = b = 131.1, c = 86.6 A	Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O28025	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Archaeoglobus fulgidus

Synonyms

Synonyms	Comment	Organism
TiaS	-	Archaeoglobus fulgidus
tRNAIle-agm2C synthetase	-	Archaeoglobus fulgidus

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Release 2023.1 (January 2023)