Title :
A synchrotron design for macromolecular structure determination
Author :
Lidestri, Joseph P.
Author_Institution :
Dept. of Biochem. & Molecular Biophys., Columbia Univ., New York, NY, USA
Abstract :
A 2.5 GeV 200 mA synchrotron has been conceptually designed with superconducting bend magnets and superconducting RF cavities. The preliminary design optimizes the synchrotron parameters for protein structure determination by considering both the acceptance phase space and the radiation flux limit of atypical protein crystal. By exploiting 5 Tesla superconducting dipoles and 500 MHz superconducting RF cavities the synchrotron can be facilitated within a 20 meter diameter. The periodic magnet lattice utilizes 8 double bend achromat (DBA) cells to produce an X-ray source with a brightness typical of second generation storage rings. The synchrotron radiation from the 5 Tesla bends would have a spectral brightness of 2.1×1014 photons/s/mr2/mm2/(0.1%bandwidth) at the K-edge of selenium which is well suited for multiwavelength anomalous diffraction (MAD) measurements
Keywords :
X-ray production; accelerator RF systems; accelerator cavities; accelerator magnets; electron accelerators; macromolecules; molecular configurations; proteins; storage rings; superconducting magnets; synchrotrons; 2.5 GeV; 20 m; 200 mA; 5 T; 500 MHz; Se; X-ray source; acceptance phase space; double bend achromat; macromolecular structure determination; multiwavelength anomalous diffraction; periodic magnet lattice; preliminary design; protein structure; second generation storage rings; superconducting RF cavities; superconducting bend magnets; superconducting dipoles; synchrotron design; Biomedical optical imaging; Brightness; Crystallography; Molecular biophysics; Proteins; Radio frequency; Space charge; Superconducting magnets; Synchrotron radiation; X-ray diffraction;
Conference_Titel :
Particle Accelerator Conference, 2001. PAC 2001. Proceedings of the 2001
Conference_Location :
Chicago, IL
Print_ISBN :
0-7803-7191-7
DOI :
10.1109/PAC.2001.987902