Literature summary extracted from

Zaccai, N.; Carter, L.; Berrow, N.; Sainsbury, S.; Nettleship, J.; Walter, T.; Harlos, K.; Owens, R.; Wilson, K.; Stuart, D.; Esnouf, R.
Crystal structure of a 3-oxoacyl-(acyl carrier protein) reductase (BA3989) from Bacillus anthracis at 2.4 A resolution (2008), Proteins Struct. Funct. Genet., 70, 562-567.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.1.1.100	PCR product recombined with pDONR221 and insert from this vector transferred in the LR reaction to the expression vector pET15g which adds a histidine tag and a 3C protease cleavage site, expressed in Escherichia coli B834(DE3) cells	Bacillus anthracis

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.1.1.100	at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates	Bacillus anthracis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.100	Bacillus anthracis	Q81JG6	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.1.1.100	by nickel-affinity chromatography	Bacillus anthracis

Subunits

EC Number	Subunits	Comment	Organism
1.1.1.100	tetramer	crystallography	Bacillus anthracis

Synonyms

EC Number	Synonyms	Comment	Organism
1.1.1.100	3-oxoacyl-(acyl carrier protein) reductase	-	Bacillus anthracis

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Release 2023.1 (January 2023)