Crystallization and preliminary X-ray studies of purine nucleoside phosphorylase from Cellulomonas sp.
The commercially available enzyme purine nucleoside phosphorylase (PNP) from Cellulomonas sp. was purified by ion--exchange chromatography, partially sequenced and crystallized in two different crystal forms using the hanging-drop vapour-diffusion technique. Crystal form A grows as polyeders and/or cubes in the cubic space group P4232 with unit-cell dimension a = 162.5 A. Crystal form B appears as thick plates in the space group P212121 with unit-cell dimensions a = 63.2, b = 108.3 and c = 117.4 A. Both crystal forms contain three monomers (one trimer) in the asymmetric unit.
Department of Biophysics, Institute of Experimental Physics, University of Warsaw, Zwirki i Wigury 93, 02-089 Warsaw, Poland.
A
A
Bzowska
J
J
Tebbe
M
M
Luić
B
B
Wielgus-Kutrowska
W
W
Schröder
D
D
Shugar
W
W
Saenger
G
G
Koellner
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D006093:Gram-Positive Asporogenous Rods / Q000201:enzymology*; D011487:Protein Conformation; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry* / Q000302:isolation & purification; D017421:Sequence Analysis
D001426:Bacterial Proteins; D011683:Purine-Nucleoside Phosphorylase