Literature summary for 3.6.1.7 extracted from

Nishibori, E.; Nakamura, T.; Arimoto, M.; Aoyagi, S.; Ago, H.; Miyano, M.; Ebisuzaki, T.; Sakata, M.
Application of maximum-entropy maps in the accurate refinement of a putative acylphosphatase using 1.3 A X-ray diffraction data (2008), Acta Crystallogr. Sect. D, 64, 237-247.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of TT0497 in Escherichia coli strain BL21(DE3)	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant TT0497, 0.0005 ml of 2.9 mg/ml protein in 20 mM Tris-HCl pH 8.0, 0.2 M NaCl is mixed with 0.0005 ml of precipitant solution containing 27.5% w/v PEG 4000 and 0.1 M MES, pH 6.9, X-ray diffraction structure determination and analysis at 1.3 A resolution, structural refinement based on the Fourier method, modelling, overview	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SKS6	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	Q5SKS6	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant TT0497 from Escherichia coli strain BL21(DE3) by two steps of ion exchange chromatography, and gel filtration	Thermus thermophilus

Subunits

Subunits	Comment	Organism
More	structure modelling, multiple conformations of the side chains of amino-acid residues	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
TT0497	-	Thermus thermophilus

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Release 2023.1 (January 2023)