z-logo
Premium
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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom