Open AccessThe purification, crystallization and preliminary structural characterization of human MAWDBP, a member of the phenazine biosynthesis‐like protein family
Author(s) -
Herde Petra,
Blankenfeldt Wulf
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106015648
Subject(s) - phenazine , crystallization , biosynthesis , characterization (materials science) , crystallography , chemistry , biochemistry , materials science , organic chemistry , gene , nanotechnology
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 m M KF, 14%( w / v ) PEG 3350 and 0.1 M sodium citrate pH 5.4. Crystals belong to space group H 32, with unit‐cell parameters a = b = 187, c = 241 Å, 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 Å resolution.