Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri.
In eukaryotes and some bacteria, the third step of reductive pyrimidine catabolism is catalyzed by beta-alanine synthase (EC 3.5.1.6). Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri were obtained using sodium citrate as a precipitant. The crystals belong to space group P2(1) (unit-cell parameters a = 117.2, b = 77.1, c = 225.5 A, beta = 95.0 degrees ) and contain four homodimers per asymmetric unit. Data were collected to 2.7 A resolution. Introduction of heavy atoms into the crystal lattice induced a different set of unit-cell parameters (a = 61.0, b = 77.9, c = 110.1 A, beta = 97.2 degrees ) in the same space group P2(1), with only one homodimer per asymmetric unit.
Dobritzsch
Doreen
D
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. doreen@alfa.mbb.ki.se
Gojković
Zoran
Z
Andersen
Birgit
B
Piskur
Jure
J
D000581:Amidohydrolases / Q000737:chemistry*; D002951:Citrates; D003460:Crystallization / Q000379:methods; D011994:Recombinant Proteins; D012440:Saccharomyces / Q000201:enzymology*; D000077559:Sodium Citrate; D014961:X-Ray Diffraction / Q000379:methods
D002951:Citrates; D011994:Recombinant Proteins; D000077559:Sodium Citrate; D000581:Amidohydrolases; C021590:beta-ureidopropionase