Literature DB >> 8749855

Crystallization and preliminary X-ray crystallographic analysis of ImmE7 protein of colicin E7.

W Y Ku1, C S Wang, C Y Chen, K F Chak, M K Safo, H S Yuan.   

Abstract

The ImmE7 protein, which can bind specifically to the DNase colicin E7 and neutralize its bactericidal activity, has been purified and crystallized in two different crystal forms by vapor diffusion method. The orthorhombic crystals belong to space group I222 or I2(1)2(1)2(1) and have unit cell dimensions a = 75.1 A, b = 50.5 A, and c = 45.4 A. The second form is monoclinic space group P2(1) with cell dimensions a = 29.3 A, b = 102.7 A, c = 53.0 A, and beta = 91.5 degrees. The orthorhombic crystals diffract to 1.8 A resolution, and are suitable for high-resolution X-ray analysis.

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Year:  1995        PMID: 8749855     DOI: 10.1002/prot.340230414

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  2 in total

1.  A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity.

Authors:  C A Dennis; H Videler; R A Pauptit; R Wallis; R James; G R Moore; C Kleanthous
Journal:  Biochem J       Date:  1998-07-01       Impact factor: 3.857

2.  The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.

Authors:  K F Chak; M K Safo; W Y Ku; S Y Hsieh; H S Yuan
Journal:  Proc Natl Acad Sci U S A       Date:  1996-06-25       Impact factor: 11.205

  2 in total

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