Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein fromEscherichia coli
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference18 articles.
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1. Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK;The International Journal of Biochemistry & Cell Biology;2007
2. Not all J domains are created equal: Implications for the specificity of Hsp40-Hsp70 interactions;Protein Science;2005-07
3. Crystal Structure of Hsc20, a J-type Co-chaperone from Escherichia coli;Journal of Molecular Biology;2000-12
4. Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichiacoli;Proceedings of the National Academy of Sciences;2000-06-27
5. Additives for the crystallization of proteins and nucleic acids;Journal of Crystal Growth;1999-01
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