title: Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus.
abstract: Phosphopentomutases (PPMs) interconvert D-ribose 5-phosphate and alpha-D-ribose 1-phosphate to link glucose and nucleotide metabolism. PPM from Bacillus cereus was overexpressed in Escherichia coli, purified to homogeneity and crystallized. Bacterial PPMs are predicted to contain a di-metal reaction center, but the catalytically relevant metal has not previously been identified. Sparse-matrix crystallization screening was performed in the presence or absence of 50 mM MnCl(2). This strategy resulted in the formation of two crystal forms from two chemically distinct conditions. The crystals that formed with 50 mM MnCl(2) were more easily manipulated and diffracted to higher resolution. These results suggest that even if the catalytically relevant metal is not known, the crystallization of putative metalloproteins may still benefit from supplementation of the crystallization screens with potential catalytic metals.
authors.affiliation: Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
authors.forename: Timothy D
authors.initials: TD
authors.lastname: Panosian
authors.forename: David P
authors.initials: DP
authors.lastname: Nannemann
authors.forename: Brian O
authors.initials: BO
authors.lastname: Bachmann
authors.forename: T M
authors.initials: TM
authors.lastname: Iverson
mesh_terms: D001409:Bacillus cereus / Q000201:enzymology*; D002712:Chlorides / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D017895:Manganese Compounds / Q000737:chemistry; D012267:Ribosemonophosphates / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D002712:Chlorides; D017895:Manganese Compounds; D012267:Ribosemonophosphates; C025340:manganese chloride