title: The purification, crystallization and preliminary structural characterization of human MAWDBP, a member of the phenazine biosynthesis-like protein family.
abstract: MAWDBP is the only representative of the phenazine biosynthesis-like protein family in the human genome. Its expression is elevated in several disease processes, including insulin resistance, folate deficiency and hypotension, and it may also be involved in carcinogenesis. The exact molecular function of MAWDBP is unknown. Native and seleno-L-methionine-labelled MAWDBP were expressed in Escherichia coli and crystallized at room temperature from precipitants containing 10 mM KF, 14%(w/v) PEG 3350 and 0.1 M sodium citrate pH 5.4. Crystals belong to space group H32, with unit-cell parameters a = b = 187, c = 241 A, indicative of three to five monomers per asymmetric unit. Crystals were cryoprotected with 15%(v/v) glycerol and data have been collected to 2.7 A resolution.
authors.affiliation: Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
authors.forename: Petra
authors.initials: P
authors.lastname: Herde
authors.forename: Wulf
authors.initials: W
authors.lastname: Blankenfeldt
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D011506:Proteins; D018036:Selenium Compounds; D012997:Solvents; D014961:X-Ray Diffraction
chemical_list: C434327:PBLD protein, human; D011506:Proteins; D018036:Selenium Compounds; D012997:Solvents; D006899:Mixed Function Oxygenases