Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA.
A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype O:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 A, and diffract to 1.55 A resolution on a synchrotron-radiation source.
Nummelin
Heli
H
Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, PO Box 65, FIN-00014 University of Helsinki, Finland.
El Tahir
Yasmin
Y
Ollikka
Pauli
P
Skurnik
Mikael
M
Goldman
Adrian
A
D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry*; D003094:Collagen / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D011487:Protein Conformation; D015007:Yersinia / Q000737:chemistry*
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; C064832:YadA protein, Yersinia; D003094:Collagen