MOTIVATION: The identification of suitable conditions for crystallization is a rate-limiting step in protein structure determination. The pH of an experiment is an important parameter and has the potential to be used in data-mining studies to help reduce the number of crystallization trials required. However, the pH is usually recorded as that of the buffer solution, which can be highly inaccurate. RESULTS: Here, we show that a better estimate of the true pH can be predicted by considering not only the buffer pH but also any other chemicals in the crystallization solution. We use these more accurate pH values to investigate the disputed relationship between the pI of a protein and the pH at which it crystallizes. AVAILABILITY AND IMPLEMENTATION: Data used to generate models are available as Supplementary Material. CONTACT: [email protected] SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Motion estimation in video is a very important tool for such applications as interpolation, motion compensation, and segmentation. However, in interlaced video, it is often desirable to perform interpolation prior to the motion estimation. In this correspondence, a novel technique is presented that, rather than minimizing the interpolation error in each of the frames used for motion estimation, seeks to make these errors equal. The new method is shown to perform deinterlacing better than several other approaches also based on Bayesian estimation.