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Purification, crystallization and preliminary X-ray crystallographic analysis of the receiver and stalk domains (PA3346RS) of the response regulator PA3346 from Pseudomonas aeruginosa PAO1
Journal article   Open access   Peer reviewed

Purification, crystallization and preliminary X-ray crystallographic analysis of the receiver and stalk domains (PA3346RS) of the response regulator PA3346 from Pseudomonas aeruginosa PAO1

Pei-Hsiu Wu, Jye-Jin Hsu, Ting-Wei Chiang, Yin-Cheng Hsieh, Hwan-You Chang, Shou-Lin Chang and Chun-Jung Chen
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol.67(8), pp.937-940
08/2011

Abstract

Pseudomonas aeruginosa receiver domain response regulator stalk domain
The regulatory domain (PA3346RS), comprising the receiver and stalk domains, of the response regulator PA3346 requires phosphorylation for activation with magnesium ions as cofactors in order to modulate the downstream protein phosphatase activity for the regulation of swarming motility in Pseudomonas aeruginosa PAO1. Fusion-tagged recombinant PA3346RS of total molecular mass 25.3 kDa has been overexpressed in Escherichia coli, purified using Ni 2+ -NTA and Q - Sepharose ion-exchange columns and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from PA3346RS crystals to 2.0 Å resolution. The crystal belonged to space group P4 1 or P4 3 , with unit-cell parameters a = 82.38, c = 73.34 Å. Preliminary analysis indicated the presence of a dimer of PA3346RS in the asymmetric unit, with a solvent content of 48.6%. © 2011 International Union of Crystallography All rights reserved.
url
https://doi.org/10.1107/S1744309111023931View
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