Crystallographic analysis of Eisenia hydrolysis-enhancing protein using a long wavelength for native-SAD phasing

In this study, EHEP was purified from the natural digestive fluid of A. kurodai and was crystallized using the sitting-drop vapor-diffusion method. Native and SAD (single-wavelength anomalous diffraction) data sets were successfully collected at resolutions of 1.20 and 2.48   Å using wavelengths of 1.0 and 2.1   Å , respectively, from crystals obtained in initial screening. The crystals belonged to space group P212121 and contained one EHEP molecule in the asymmetric unit. All 20 S-atom sites in EHEP were located and the phases were determined by the SAD method using the S atoms in the natural protein as anomalous scatterers (native-SAD). After phase improvement, interpretable electron densities were obtained and 58% of the model was automatically built.

Source: Acta Crystallographica Section F - December 24, 2019 Category: Biochemistry Authors: Sun, X. Ye, Y. Sakurai, N. Kato, K. Yuasa, K. Tsuji, A. Yao, M. Tags: EHEP phlorotannin binding solutionless crystal mount native-SAD biofuel research communications Source Type: research