Nucleation induction times of the protein lysozyme in aqueous solution were studied using electrodynamic levitation of single solution droplets. This technique allows the study of homogeneous nucleation by the elimination of dust, dirt, and container walls. A new experimental procedure was employed, which allowed control of the relative humidity around the supersaturated droplet and thus allowed the measurement of nucleation induction time at a given supersaturation. This measurement was performed 510 times at essentially identical conditions to obtain sufficient data to examine the statistics of nucleation induction time. An analysis of the data using the classic approach of Turnbull and a newly proposed two-step treatment is presented.