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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.7 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

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

Purification (Commentary)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 TT0497
-
Thermus thermophilus