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Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)

Disulfide‐bond (Dsb) proteins are a family of redox proteins containing a Cys‐X‐X‐Cys motif. They are essential for disulfide‐bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for...

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Published in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-09, Vol.57 (9), p.1293-1295
Main Authors:	Edeling, Melissa A., Guddat, Luke W., Fabianek, Renata A., Halliday, Judy A., Jones, Alun, Thöny-Meyer, Linda, Martin, Jennifer L.
Format:	Article
Language:	English
Subjects:	Amino Acid Substitution Bradyrhizobium - chemistry Crystallization Crystallography, X-Ray cytochrome c maturation disulfide oxidoreductase Dsb proteins Oxidoreductases - biosynthesis Oxidoreductases - chemistry Oxidoreductases - genetics Periplasmic Proteins Protein Conformation Selenomethionine - chemistry
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container_title	Acta crystallographica. Section D, Biological crystallography.
container_volume	57
creator	Edeling, Melissa A. Guddat, Luke W. Fabianek, Renata A. Halliday, Judy A. Jones, Alun Thöny-Meyer, Linda Martin, Jennifer L.
description	Disulfide‐bond (Dsb) proteins are a family of redox proteins containing a Cys‐X‐X‐Cys motif. They are essential for disulfide‐bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X‐rays to 1.14 Å resolution. The crystals are orthorhombic, space group P212121, with unit‐cell parameters a = 35.1, b = 48.2, c = 90.2 Å. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine‐pathway inhibition and was purified without reducing agents.
doi_str_mv	10.1107/S0907444901009982
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source	Wiley-Blackwell Read & Publish Collection; Alma/SFX Local Collection
subjects	Amino Acid Substitution Bradyrhizobium - chemistry Crystallization Crystallography, X-Ray cytochrome c maturation disulfide oxidoreductase Dsb proteins Oxidoreductases - biosynthesis Oxidoreductases - chemistry Oxidoreductases - genetics Periplasmic Proteins Protein Conformation Selenomethionine - chemistry
title	Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE)
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