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Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis
Authors:Christoph?Scheich  author-information"  >  author-information__contact u-icon-before"  >  mailto:scheich@molgen.mpg.de"   title="  scheich@molgen.mpg.de"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Dietmar?Leitner,Volker?Sievert,Martina?Leidert,Brigitte?Schlegel,Bernd?Simon,Ivica?Letunic,Konrad?Büssow,Anne?Diehl
Affiliation:1.Proteinstrukturfabrik,Berlin,Germany;2.Max Planck Institut für Molekulare Genetik,Berlin,Germany;3.Forschungsinstitut für Molekulare Pharmakologie,Berlin,Germany;4.European Molecular Biology Laboratory (EMBL),Heidelberg,Germany
Abstract:

Background  

High-throughput protein structure analysis of individual protein domains requires analysis of large numbers of expression clones to identify suitable constructs for structure determination. For this purpose, methods need to be implemented for fast and reliable screening of the expressed proteins as early as possible in the overall process from cloning to structure determination.
Keywords:
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