Literature summary for 2.8.1.12 extracted from

Kanaujia, S.P.; Ranjani, C.V.; Jeyakanthan, J.; Ohmori, M.; Agari, K.; Kitamura, Y.; Baba, S.; Ebihara, A.; Shinkai, A.; Kuramitsu, S.; Shiro, Y.; Sekar, K.; Yokoyama, S.
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of molybdopterin synthase from Thermus thermophilus HB8 (2007), Acta Crystallogr. Sect. F, 63, 324-326.

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified MoaB, sitting drop vapour diffusion method, 0.001 ml of 11 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, are mixed with 0.001 ml of well solution containing 20% w/v PEG 3350, and 0.2 M tripotassium citrate monohydrate, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 1.64 A resolution	Thermus thermophilus

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
recombinaant MoaB from Escherichia coli strain BL21(DE3) by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, anion and cation exchange chromatography, an hydroxyapatite chromatography	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
MoaB	-	Thermus thermophilus
TTHA0341	-	Thermus thermophilus

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Release 2023.1 (January 2023)