US-France Cooperative Research:  New X-ray Techniques to    Study Ligation State Changes in Aminoacyl-tRNA Synthetases
{'Code': '01090000', 'Directorate': {'Abbreviation': 'O/D', 'LongName': 'Office Of The Director'}, 'Division': {'Abbreviation': 'OISE', 'LongName': 'Office Of Internatl Science &Engineering'}}
{'SignBlockName': 'Pierre Perrolle', 'PO_EMAI': None, 'PO_PHON': None}
This award will support collaborative research between Dr. Charles              W. Carter, University of North Carolina at Chapel Hill and Dr.                  Charles Zelwer, Centre de Genetique Moleculaire, Gif-sur-Yvette,                France.  Drs. Carter and Zelwer are presently involved in a project             on the topic of three-dimensional structures of aminoacyl-tRNA                  synthetases.  Their groups are working on enzymes for two different             amino acids:  Dr. Carter on the tryptophanyl enzyme from B.                     stearothermophilus and Dr. Zelwer on the methionyl enzyme from E.               coli.  The investigators each have different areas of expertise                 with data collection and phase determination methods and the                    proposed project will benefit from a combination of their                       experiences and resources.                                                                                                                                      In this project, Drs. Carter and Zelwer plan 1) to cooperate on                 implementing and testing programs for an empirical absorption                   correction method for use in collected X-ray intensity data using               three-circle goniometry and a two-dimensional area detector; 2) to              complete data collection on a series of native and liganded form II             methionyl-tRNA synthetase crystals; 3) to collect high resolution               synchrotron data from one form of the tryptophanyl enzyme, and                  4) to compare differences and similarities between different                    conformations of the two aminoacyl-tRNA synthetases.  The results               of this research will contribute to our understanding of                        aminoacyl-tRNA synthetases; these enzymes supervise translation of              the genetic code by virtue of their ability to recognize and                    assemble specifically the twenty amino acids and their                          cognatetransfer RNA molecules.
{'FirstName': 'Charles', 'LastName': 'Carter', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': 'Jr.', 'PI_FULL_NAME': 'Charles W Carter', 'EmailAddress': 'carter@med.unc.edu', 'NSF_ID': '000102154', 'StartDate': '02/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of North Carolina at Chapel Hill', 'CityName': 'CHAPEL HILL', 'ZipCode': '275995023', 'PhoneNumber': '9199663411', 'StreetAddress': '104 AIRPORT DR STE 2200', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'NC04', 'ORG_UEI_NUM': 'D3LHU66KBLD5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF NORTH CAROLINA AT CHAPEL HILL', 'ORG_PRNT_UEI_NUM': 'N8DMK1K4C2K5'}
{'Name': 'University of North Carolina School of Medicine', 'CityName': 'Chapel Hill', 'StateCode': 'NC', 'ZipCode': '27514', 'StreetAddress': '300 Bynum Hall, 008a', 'CountryCode': 'US', 'CountryName': 'United States', 'StateName': 'North Carolina', 'CountryFlag': '1', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_PERF': 'NC04'}
{'Code': '5918', 'Text': 'FRANCE'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8815367.xml'}