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Native sulfur/chlorine SAD phasing for serial femtosecond crystallography
Takanori Nakane1, Changyong Song2, Mamoru Suzuki2
1Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Acta Crystallographica. Section D, Biological Crystallography
|December 3, 2015
Summary
Serial femtosecond crystallography (SFX) can now determine native protein structures using sulfur single-wavelength anomalous diffraction (SAD). This sulfur SAD method advances native crystal structure determination, overcoming previous limitations in SFX phasing.
Area of Science:
- Structural Biology
- Biophysics
- Crystallography
Background:
- Serial femtosecond crystallography (SFX) minimizes radiation damage for protein structure determination.
- Phasing native crystals using SFX remains a significant challenge.
- Anomalous diffraction methods are crucial for solving crystal structures.
Purpose of the Study:
- To demonstrate the feasibility of phasing native crystals using single-wavelength anomalous diffraction (SAD) in SFX.
- To utilize the anomalous signal from sulfur and chlorine atoms for phasing.
- To establish a new method for native crystal structure determination in SFX.
Main Methods:
- Serial femtosecond crystallography (SFX) was employed.
- Single-wavelength anomalous diffraction (SAD) was performed at 1.77 Å.
- The anomalous signal from sulfur and chlorine in native lysozyme crystals was exploited.
Main Results:
- Successful structure determination of native lysozyme was achieved using sulfur SAD.
- The anomalous signal from sulfur and chlorine atoms was effectively utilized for phasing.
- The demonstrated method shows promise for phasing other native protein crystals.
Conclusions:
- Sulfur SAD is a viable method for phasing native crystals in SFX.
- This technique broadens the applicability of SFX for native protein structure determination.
- The sulfur SAD approach is expected to improve the efficiency of solving native crystal structures.
