title: Crystallization and preliminary X-ray crystallographic analysis of Ace: a collagen-binding MSCRAMM from Enterococcus faecalis.
abstract: 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.
authors: School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294-0005, USA.
authors: Karthe
authors: K
authors: Ponnuraj
authors: Yi
authors: Y
authors: Xu
authors: Dwight
authors: D
authors: Moore
authors: Champion C S
authors: CC
authors: Deivanayagam
authors: Lluis
authors: L
authors: Boque
authors: Magnus
authors: M
authors: Hook
authors: Sthanam V L
authors: SV
authors: Narayana
mesh_terms: 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*
chemical_list: C121675:Ace protein, Enterococcus; D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D002352:Carrier Proteins; C048165:adhesin, Staphylococcus aureus