Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus.
Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4'-phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty-acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 A, respectively. Full sets of X-ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.
Daubaras
Dayna L
DL
Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, New Jersey 07033, USA.
Wilson
Eileen M
EM
Black
Todd
T
Strickland
Corey
C
Beyer
Brian M
BM
Orth
Peter
P
D001426:Bacterial Proteins / Q000737:chemistry; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D011092:Polyethylene Glycols; D012965:Sodium Chloride; D012997:Solvents; D013211:Staphylococcus aureus / Q000201:enzymology*; D017855:Transferases (Other Substituted Phosphate Groups) / Q000737:chemistry*
D001426:Bacterial Proteins; D012997:Solvents; D011092:Polyethylene Glycols; D012965:Sodium Chloride; D017855:Transferases (Other Substituted Phosphate Groups); C021364:holo-(acyl-carrier-protein) synthase