Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.
Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.
School of Molecular and Biomedical Sciences, University of Adelaide, North Terrace, Adelaide SA 5005, Australia.
Nicole R
NR
Pendini
Steve W
SW
Polyak
Grant W
GW
Booker
John C
JC
Wallace
Matthew C J
MC
Wilce
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D001710:Biotin / Q000737:chemistry* / Q000235:genetics; D019921:Biotinylation; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006639:Histidine / Q000737:chemistry; D008970:Molecular Weight; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013211:Staphylococcus aureus / Q000201:enzymology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D006639:Histidine; D001710:Biotin; D019731:Carbon-Nitrogen Ligases