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Expression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR protein.

ABSTRACT: Pseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 A. The crystals belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 118.8, b = 118.8, c = 495.1 A, alpha = beta = 90, gamma = 120 degrees .

SUBMITTER: Kotaka M 

PROVIDER: S-EPMC2765895 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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Expression, purification and preliminary crystallographic analysis of Pseudomonas aeruginosa RocR protein.

Kotaka Masayo M   Dutta Sujit S   Lee Hooi Chen HC   Lim Mitchell J M MJ   Wong Yeehwa Y   Rao Feng F   Mitchell Edward P EP   Liang Zhao Xun ZX   Lescar Julien J  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090925 Pt 10

Pseudomonas aeruginosa RocR, an EAL-domain protein which regulates the expression of virulence genes and biofilm formation, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of RocR are reported. The X-ray diffraction data were processed to a resolution of 2.50 A. The crystals belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 118.8, b = 118.8, c = 495.1 A, alpha = beta = 90, gamma = 120 degrees . ...[more]

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