Karthe Ponnuraj , Yi Xu , Dwight Moore , Champion C.S. Deivanayagam , Lluis Boque , Magnus Hook , Sthanam V.L. Narayana
{"title":"粪肠球菌胶原结合基质Ace的结晶及初步x射线晶体学分析","authors":"Karthe Ponnuraj , Yi Xu , Dwight Moore , Champion C.S. Deivanayagam , Lluis Boque , Magnus Hook , Sthanam V.L. Narayana","doi":"10.1016/S0167-4838(01)00328-4","DOIUrl":null,"url":null,"abstract":"<div><p>Ace is a collagen-binding bacterial cell surface adhesin from <em>Enterococcus faecalis</em>. 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 Å data set has been collected on the orthorhombic crystal form with unit cell parameters <em>a</em>=38.43 <em>b</em>=48.91 and <em>c</em>=83.73 Å. Ace40 was crystallized in the trigonal space group P3<sub>1</sub>21 or P3<sub>2</sub>21 with unit cell parameters <em>a</em>=<em>b</em>=80.24, <em>c</em>=105.91 Å; <em>α</em>=<em>β</em>=90 and <em>γ</em>=120°. A full set of X-ray diffraction data was collected to 2.5 Å. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":"1596 2","pages":"Pages 173-176"},"PeriodicalIF":0.0000,"publicationDate":"2002-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(01)00328-4","citationCount":"11","resultStr":"{\"title\":\"Crystallization and preliminary X-ray crystallographic analysis of Ace: a Collagen-binding MSCRAMM from Enterococcus faecalis\",\"authors\":\"Karthe Ponnuraj , Yi Xu , Dwight Moore , Champion C.S. Deivanayagam , Lluis Boque , Magnus Hook , Sthanam V.L. Narayana\",\"doi\":\"10.1016/S0167-4838(01)00328-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Ace is a collagen-binding bacterial cell surface adhesin from <em>Enterococcus faecalis</em>. 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 Å data set has been collected on the orthorhombic crystal form with unit cell parameters <em>a</em>=38.43 <em>b</em>=48.91 and <em>c</em>=83.73 Å. Ace40 was crystallized in the trigonal space group P3<sub>1</sub>21 or P3<sub>2</sub>21 with unit cell parameters <em>a</em>=<em>b</em>=80.24, <em>c</em>=105.91 Å; <em>α</em>=<em>β</em>=90 and <em>γ</em>=120°. A full set of X-ray diffraction data was collected to 2.5 Å. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.</p></div>\",\"PeriodicalId\":100166,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology\",\"volume\":\"1596 2\",\"pages\":\"Pages 173-176\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2002-04-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0167-4838(01)00328-4\",\"citationCount\":\"11\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0167483801003284\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0167483801003284","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
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 Å data set has been collected on the orthorhombic crystal form with unit cell parameters a=38.43 b=48.91 and c=83.73 Å. Ace40 was crystallized in the trigonal space group P3121 or P3221 with unit cell parameters a=b=80.24, c=105.91 Å; α=β=90 and γ=120°. A full set of X-ray diffraction data was collected to 2.5 Å. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.