The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus
The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export‐related activities. Here we report the 2.0 Å‐resolution crystal structure of the Thermus thermophilus CsaA protein, designated ttCsaA. Atomic structure and experiments in solution revealed a homodimer...
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Published in | The EMBO journal Vol. 20; no. 3; pp. 562 - 569 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
01.02.2001
Blackwell Publishing Ltd Oxford University Press |
Subjects | |
Online Access | Get full text |
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