Crystallization and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter haemolysin B

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 67, Issue 5, 2011, Pages 630-633

  Schwarz, Christian K W ^a   Tschapek, Britta ^a   Jumpertz, Thorsten ^a   Jenewein, Stefan ^a   Lecher, Justin ^a,b   Willbold, Dieter ^a,b   Panjikar, Santosh ^c   Holland, I Barry ^d   Smits, Sander H J ^a   Schmitt, Lutz ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b FORSCHUNGSZENTRUM JÜLICH   (Germany)

^c DESY   (Germany)

^d UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

buffer screens; C39 peptidases; haemolysins; inclusion bodies; oligomers; refolding; type I secretion systems

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; CARRIER PROTEIN; HEMOLYSIN; HLYB PROTEIN, BACTERIA;

ARTICLE; CHEMISTRY; CRYSTALLIZATION; ESCHERICHIA COLI; PROTEIN MULTIMERIZATION; PROTEIN REFOLDING; X RAY CRYSTALLOGRAPHY;

ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; CARRIER PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HEMOLYSIN PROTEINS; PROTEIN MULTIMERIZATION; PROTEIN REFOLDING;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 79955667861     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309111010876     Document Type: Article

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