Abstract
The basic pancreatic trypsin inhibitor (abbreviated in the following as PTI) is one of the first natural proteinase inhibitors described in the literature [1–2]. Its amino acid sequence was determined simultaneously by several groups [3–6]. In 1970 the tertiary structure of PTI was reported by Huber et al [7, 17]. A model was built on the basis of an electron density map at 2.5 Å resolution, calculated from observed structure factor amplitudes and multiple isomorphous replacement phases. The purpose of this paper is to describe the crystallographic refinement at 1.5 Å resolution of the PTI model and to present results which have been obtained from the refined model.
Supported by Deutsche Forschungsgemeinschaft and SFB 51.
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Deisenhofer, J., Steigemann, W. (1974). The Model of the Basic Pancreatic Trypsin Inhibitor Refined at 1.5 Å Resolution. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_54
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DOI: https://doi.org/10.1007/978-3-642-87966-1_54
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