Crystallization and preliminary crystallographic analysis of a new crystal form of arylsulfatase A isolated from human placenta.
Depending on pH, arylsulfatase A exists in solution as a dimer or as an octamer. The enzyme isolated from human placenta was crystallized at pH 5.4 in a new crystal form with space group C2, unit-cell parameters a = 154.0, b = 190.3, c = 112.5 A, beta = 122.4 degrees and four subunits in the asymmetric unit. At pH 6.5-6.7, tetragonal crystals are obtained that are isomorphous to the known crystals of recombinant arylsulfatase A obtained at pH 5.0-5.4. The crystal structure of both forms was determined by the molecular-replacement method. The monoclinic crystals contain octamers of the same type as found in the tetragonal form.
Lewinski
K
K
Faculty of Chemistry, Jagiellonian University, 30-060 Kraków, Poland. lewinski@chemia.uj.edu.pl
Chruszcz
M
M
Ksiazek
D
D
Laidler
P
P
D002553:Cerebroside-Sulfatase / Q000737:chemistry* / Q000302:isolation & purification; D003196:Computer Graphics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D019281:Dimerization; D005260:Female; D006801:Humans; D008958:Models, Molecular; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D002553:Cerebroside-Sulfatase