STRUCTURE BASED APPROACH TO ISSUES IN ZINC FINGER RECOGNITION

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Aart is a six-finger zinc finger protein designed by Prof. David Segal in the Barbas lab at the Scripps Research Institute. It is an excellent choice for crystallographic studies because several of the nucleotide triads it binds are unusual and because it may offer insight into the strain associated with zinc finger proteins longer than three fingers in length. The protein has been crystallized in this lab previously. A complete native data set has been collected to 2.95 ¿¿at APS BL 14-BMC (P1 a = 40.57 ¿¿b = 69.09 ¿¿c = 70.84 ¿¿alpha = 101.18¿¿ beta = 94.36¿¿ gamma = 105.30¿¿) there are two protein molecules and two twenty-two base pair DNA duplexes in the asymmetric unit. Synchrotron radiation is necessary for high resolution data collection as well as structure solution. Multi wavelength anomalous dispersion data collection is planned using brominated DNA derivatives of this crystal form.