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International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 4(59), p. 758-760, 2003

DOI: 10.1107/s090744490300372x

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Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

This paper is available in a repository.
This paper is available in a repository.

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Preprint: archiving allowed
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Postprint: archiving allowed
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Published version: archiving allowed
Data provided by SHERPA/RoMEO

Abstract

MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.