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The Berkeley Center for Structural Biology (BCSB) operates and develops a suite of protein crystallography beamlines at the Advanced Light Source (ALS) located at Lawrence Berkeley National Laboratory (LBNL). Although the ALS was conceived as a low-energy (1.9-GeV), third-generation synchrotron source of vacuum ultraviolet (VUV) and soft X-ray radiation, it was realized during the development of the facility in the mid-1990s that a multipole wiggler coupled with brightness-preserving optics would result in a beamline whose performance in the energy range of 5 to 15 keV would be sufficient for most protein crystallographic experiments. Later, the hard X-ray capabilities of the ALS were expanded by the addition of three superconducting bending magnets, resulting in additional protein crystallography facilities at the ALS [1].

Although the Advanced Light Source (ALS) was initially conceived primarily as a low-energy (1.9-GeV) third-generation source of vacuum ultraviolet (VUV) and soft X-ray radiation, it was realized very early in the development of the facility that a multipole wiggler source coupled with high-quality (brightness-preserving) optics would result in a beamline whose performance across the optimal energy range (5–15 keV) for macromolecular crystallography (MX) would be comparable to, or even exceed, that of many existing crystallography beamlines at higher-energy facilities. Hence, starting in 1996, a suite of three beamlines, branching off a single wiggler source, was constructed, which together formed the ALS Macromolecular Crystallography Facility [1]. From the outset, this facility was designed to cater equally to the needs of both academic and industrial users, with a heavy emphasis placed on the development and introduction of high-throughput crystallographic tools, techniques, and facilities, including la...