Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein

Ulrike C. Kühlmann; Colin Kleanthous; Richard James; Geoffrey R. Moore; Andrew M. Hemmings

doi:10.1107/S0108444998002590

Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein

Ulrike C. Kühlmann
, Colin Kleanthous
, Richard James
, Geoffrey R. Moore
, Andrew M. Hemmings

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, K(d) = 1 x 10^-16 M, reveals it to be one of the highest affinity protein-protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P2₁2₁2₁ with one molecule of complex in the asymmetric unit, and crystals contain approximately 43% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.

Original language	English
Pages (from-to)	256-259
Number of pages	4
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	1
DOIs	https://doi.org/10.1107/S0108444998002590
Publication status	Published - 1 Jan 1999

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title = "Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein",

abstract = "We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, K(d) = 1 x 10-16 M, reveals it to be one of the highest affinity protein-protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P212121 with one molecule of complex in the asymmetric unit, and crystals contain approximately 43\% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.",

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Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein. / Kühlmann, Ulrike C.; Kleanthous, Colin; James, Richard et al.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 1, 01.01.1999, p. 256-259.

Research output: Contribution to journal › Article › peer-review

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AU - Kühlmann, Ulrike C.

AU - Kleanthous, Colin

AU - James, Richard

AU - Moore, Geoffrey R.

AU - Hemmings, Andrew M.

PY - 1999/1/1

Y1 - 1999/1/1

N2 - We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, K(d) = 1 x 10-16 M, reveals it to be one of the highest affinity protein-protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P212121 with one molecule of complex in the asymmetric unit, and crystals contain approximately 43% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.

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JF - Acta Crystallographica Section D: Biological Crystallography

IS - 1

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Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein

Abstract

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