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Literature summary for 3.4.21.B57 extracted from

  • Tanaka, S.; Saito, K.; Chon, H.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
    Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon (2006), Acta Crystallogr. Sect. F, 62, 902-905.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overproduction of pro-S255A in Escherichia coli BL21-Codon-Plus(DE3) Thermococcus kodakarensis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of the active-site mutant S255A of pro-Tk-subtilisin. The crystal is grown at 4°C by the sitting-drop vapour-diffusion method. Native X-ray diffraction data are collected to 2.3 A resolution.They crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 92.69, b = 121.78, c = 77.53 A. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V(M) was calculated to be 2.6 A(3) Da(-1) and the solvent content was 53.1% Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
S255A active-site mutant enzyme Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
active-site mutant S255A of pro-Tk-subtilisin Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis P58502 sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106)
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermococcus kodakarensis

Subunits

Subunits Comment Organism
monomer 1 * 45000, active-site mutant S255A of pro-Tk-subtilisin, SDS-PAGE Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
Tk-subtilisin
-
Thermococcus kodakarensis