MAD Phase Assignment
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky', 'PO_EMAI': None, 'PO_PHON': None}
This project involves both experimental and theoretical                         components.  Multiple-wavelength diffraction data will be                       collected from a number of protein crystals selected for both                   the biological interest in the protein structures and the                       suitability for further developing the MAD phasing technique.                   This data will be collected at the Stanford Synchrotron                         Radiation Laboratory.  Structure determination will proceed                     using MAD phase assignment and conventional crystallographic                    techniques.  Refinements and extensions to the currently                        implemented MAD phasing algorithms will be developed in the                     course of the work.  Drs. Merritt and Adman will evaluate the                   existing and newly developed MAD phasing algorithms by                          comparison of the resulting MAD phases and electron density                     maps against the corresponding phases and maps of the                           refined crystal structures.                                                                                                                                     Multiple-Wavelength Anomalous Dispersion (MAD) phase                            assignment                                                                      has recently been used successfully to determine the structure of               several small proteins.  An outstanding advantage of this novel                 technique is that structures may be determined using diffraction                measurements from a single crystal of native protein.  The method               is based on measuring small changes in X-ray scattering amplitude               as a function of X-ray wavelength.  The eventual range of                       structure determinations for which it becomes the method of                     choice will depend on improving both experimental technique and                 data analysis to overcome the relatively small signal-to-noise                  ratio.***
[{'FirstName': 'Elinor', 'LastName': 'Adman', 'PI_MID_INIT': 'T', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Elinor T Adman', 'EmailAddress': None, 'NSF_ID': '000186291', 'StartDate': '11/01/1989', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Ethan', 'LastName': 'Merritt', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Ethan A Merritt', 'EmailAddress': None, 'NSF_ID': '000285952', 'StartDate': '11/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'University of Washington', 'CityName': 'SEATTLE', 'ZipCode': '981951016', 'PhoneNumber': '2065434043', 'StreetAddress': '4333 BROOKLYN AVE NE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Washington', 'StateCode': 'WA', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'WA07', 'ORG_UEI_NUM': 'HD1WMN6945W6', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF WASHINGTON', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1108', 'Text': 'INSTRUMENTAT & INSTRUMENT DEVP'}, {'Code': '1164', 'Text': 'MOLECULAR BIOPHYSICS'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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