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Crystallization and preliminary X‐ray crystallographic analysis of phosphoribulokinase from Rhodobacter sphaeroides
Author(s) -
Roberts David L.,
Runquist Jennifer A.,
Miziorko Henry M.,
Kim JungJa P.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041126
Subject(s) - rhodobacter sphaeroides , crystallography , crystallization , monomer , chemistry , rhodobacter , photosynthesis , polymer , biochemistry , organic chemistry , mutant , gene
A recombinant form of Rhodobacter sphaeroides phosphoribulokinase (PRK), expressed in Escherichia coli and isolated by affinity chromatography, was crystallized by the sitting drop vapor diffusion technique using NH 4 H 2 PO 4 (pH 5.6) as the precipitating agent. PRK crystallizes in the cubic space group P432, with unit cell parameters a = b = c = 129.55 Å. Based on the assumption of one 32‐kDa monomer per asymmetric unit, the V m value is 2.83 Å 3 /Da. The octameric molecular symmetry is consistent with two planar tetramers stacked in a nearly eclipsed arrangement. A native data set has been collected to 2.6 Å resolution.