| Autor: |
Chiang, Cheng‐Hung, Chou, Chung‐Kuang, Tseng, Chien‐Chang, Chen, Yi‐Hui, Liu, Yi‐Chun, Huang, Chen‐Ying, Chao, Chun‐Hsiung, Huang, Chun‐Hsiang |
| Zdroj: |
Journal of the Chinese Chemical Society; July 2024, Vol. 71 Issue: 7 p721-731, 11p |
| Abstrakt: |
Synchrotron protein crystallography (PX) remains an indispensable tool for uncovering the atomic structures of biomolecules. TLS 15A1, operated by the protein diffraction group of NSRRC, has been accessible to both academic and industrial users since January 2013. This beamline is energy‐tunable within a range between 5.6 and 15.5 keV, which is suitable for phasing experiments. Over the past 11 years, TLS 15A1 has supported 657 projects and facilitated 1523 experiments across 41,656 h of beamtime. This article describes the beamline layout, studies of factors influencing data quality, and significant scientific contributions. Photograph of the sample environment set‐up in the TLS 15A1 experimental station. The experimental station is equipped with a high precision X‐ray MD2 micro‐diffractometer, a large area CCD detector, Cryojet, and an automatic sample mounting system (SAM) for highly efficient data collection. |
| Databáze: |
Supplemental Index |
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