01481nas a2200217 4500008004100000022001400041245012500055210006900180260007400249300001200323490000700335520065300342100002100995700001901016700002101035700001801056700002501074700002001099700001901119856012501138 2005 eng d a2053-230X00aCloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis0 aCloning purification crystallization and preliminary structural a2 ABBEY SQ, CHESTER, CH1 2HU, ENGLANDbINT UNION CRYSTALLOGRAPHYcJUL a680-6830 v613 a
{Penicillin acylase proteins are amidohydrolase enzymes that cleave penicillins at the amide bond connecting the side chain to their beta-lactam nucleus. An unannotated protein from Bacillus subtilis has been expressed in Escherichia coli, purified and confirmed to possess penicillin V acylase activity. The protein was crystallized using the hanging-drop vapour-diffusion method from a solution containing 4 M sodium formate in 100 mM Tris-HCl buffer pH 8.2. Diffraction data were collected under cryogenic conditions to a spacing of 2.5 A. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.0
1 aRathinaswamy, P.1 aPundle, A., V.1 aPrabhune, Asmita1 aSivaRaman, H.1 aBrannigan, James, A.1 aDodson, Guy, G.1 aSuresh, C., G. uhttp://library.ncl.res.in/content/cloning-purification-crystallization-and-preliminary-structural-studies-penicillin-v-0