Crystallization and preliminary X-ray crystallographic analysis of Ace: a collagen-binding MSCRAMM from Enterococcus faecalis.
Ace is a collagen-binding bacterial cell surface adhesin from Enterococcus faecalis. The collagen-binding domain of Ace (termed Ace40) and its truncated form Ace19 have been crystallized by the vapor-diffusion hanging-drop method. Ace19 was crystallized in two different crystal forms. A complete 1.65 A data set has been collected on the orthorhombic crystal form with unit cell parameters a=38.43 b=48.91 and c=83.73 A. Ace40 was crystallized in the trigonal space group P3(1)21 or P3(2)21 with unit cell parameters a=b=80.24, c=105.91 A; alpha=beta=90 and gamma=120 degrees. A full set of X-ray diffraction data was collected to 2.5 A. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.
Ponnuraj
Karthe
K
School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294-0005, USA.
Xu
Yi
Y
Moore
Dwight
D
Deivanayagam
Champion C S
CC
Boque
Lluis
L
Hook
Magnus
M
Narayana
Sthanam V L
SV
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D013293:Enterococcus faecalis / Q000737:chemistry / Q000378:metabolism*
C121675:Ace protein, Enterococcus; D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D002352:Carrier Proteins; C048165:adhesin, Staphylococcus aureus