![]() When recording the X-ray images, the Bragg peaks are detected in the diffraction patterns and used to determine the crystal system and dimensions of the unit cell as well as the crystal orientation in the X-ray beam. ![]() Therefore, the proposed approach, which is based on serial crystallography, is suitable for processing multicrystal diffraction data in cryocrystallography.ĭuring a typical cryocrystallographic data collection process, the preferred approach is to mount a single crystal in the path of the X-ray beam and obtain the single-crystal diffraction patterns to determine the structure of the crystal. Using this indexed multi-lattice information, the crystal structure of the lysozyme could be determined successfully at a resolution of 1.9 Å. From 360 images containing multicrystal diffraction patterns, 1138 and 691 crystal lattices could be obtained using the XGANDALF and MOSFLM indexing algorithms, respectively. Multicrystal diffraction data were collected from lysozyme crystals and processed using the serial crystallography program CrystFEL. Here, an approach for processing multicrystal diffraction data using a serial crystallography program is introduced that allows for the integration of multicrystal diffraction patterns from a single image. The indexing of multicrystal diffraction patterns in cryocrystallography requires more precise data processing techniques and is therefore time consuming. However, the X-ray data recorded often may contain diffraction patterns from several crystals. In standard cryocrystallography, a single crystal is used for collecting diffraction data, which include single-crystal diffraction patterns. This technique uses a cryoenvironment, which significantly reduces the radiation damage to the crystals and has the advantage of requiring only one crystal for structural determination. Cryocrystallography is a widely used method for determining the crystal structure of macromolecules.
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