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The highly automated macromolecular crystallography beamline AMX/17-ID-1 is an undulator-based high-intensity (>5 - 1012 photons s-1), micro-focus (7 mm - 5 mm), low-divergence (1 mrad - 0.35 mrad) energy-tunable (5-18 keV) beamline at the NSLS-II, Brookhaven National Laboratory, Upton, NY, USA. It is one of the three life science beamlines constructed by the NIH under the ABBIX project and it shares sector 17-ID with the FMX beamline, the frontier micro-focus macromolecular crystallography beamline. AMX saw first light in March 2016 and started general user operation in February 2017. At AMX, emphasis has been placed on high throughput, high capacity, and automation to enable data collection from the most challenging projects using an intense micro-focus beam. Here, the current state and capabilities of the beamline are reported, and the different macromolecular crystallography experiments that are routinely performed at AMX/17-ID-1 as well as some plans for the near future are presented. [ABSTRACT FROM AUTHOR]

The design of an angular array of electron time‐of‐flight (eToF) spectrometers is reported, intended for non‐invasive spectral, temporal, and polarization characterization of single shots of high‐repetition rate, quasi‐continuous, short‐wavelength free‐electron lasers (FELs) such as the LCLS II at SLAC. This array also enables angle‐resolved, high‐resolution eToF spectroscopy to address a variety of scientific questions on ultrafast and nonlinear light–matter interactions at FELs. The presented device is specifically designed for the time‐resolved atomic, molecular and optical science endstation (TMO) at LCLS II. In its final version, the spectrometer comprises up to 20 eToF spectrometers aligned to collect electrons from the interaction point, which is defined by the intersection of the incoming FEL radiation and a gaseous target. The full composition involves 16 spectrometers forming a circular equiangular array in the plane normal to the X‐ray propagation and four spectrometers at 54.7° angle relative to the principle linear X‐ray polarization axis with orientations in the forward and backward direction of the light propagation. The spectrometers are capable of independent and minimally chromatic electrostatic lensing and retardation, in order to enable simultaneous angle‐resolved photo‐ and Auger–Meitner electron spectroscopy with high energy resolution. They are designed to ensure an energy resolution of 0.25 eV across an energy window of up to 75 eV, which can be individually centered via the adjustable retardation to cover the full range of electron kinetic energies relevant to soft X‐ray methods, 0–2 keV. The full spectrometer array will enable non‐invasive and online spectral‐polarimetry measurements, polarization‐sensitive attoclock spectroscopy for characterizing the full time–energy structure of SASE or seeded LCLS II pulses, and support emerging trends in molecular‐frame spectroscopy measurements. [ABSTRACT FROM AUTHOR]

Here we present two robotic sample changers integrated into the experimental stations for the macromolecular crystallography (MX) beamlines AMX and FMX, and the biological small‐angle scattering (bioSAXS) beamline LiX. They enable fully automated unattended data collection and remote access to the beamlines. The system designs incorporate high‐throughput, versatility, high‐capacity, resource sharing and robustness. All systems are centered around a six‐axis industrial robotic arm coupled with a force torque sensor and in‐house end effectors (grippers). They have the same software architecture and the facility standard EPICS‐based BEAST alarm system. The MX system is compatible with SPINE bases and Unipucks. It comprises a liquid nitrogen dewar holding 384 samples (24 Unipucks) and a stay‐cold gripper, and utilizes machine vision software to track the sample during operations and to calculate the final mount position on the goniometer. The bioSAXS system has an in‐house engineered sample storage unit that can hold up to 360 samples (20 sample holders) which keeps samples at a user‐set temperature (277 K to 300 K). The MX systems were deployed in early 2017 and the bioSAXS system in early 2019. [ABSTRACT FROM AUTHOR]

Two new macromolecular crystallography (MX) beamlines at the National Synchrotron Light Source II, FMX and AMX, opened for general user operation in February 2017 [Schneider et al. (2013). J. Phys. Conf. Ser.425, 012003; Fuchs et al. (2014). J. Phys. Conf. Ser.493, 012021; Fuchs et al. (2016). AIP Conf. Proc. SRI2015, 1741, 030006]. FMX, the micro‐focusing Frontier MX beamline in sector 17‐ID‐2 at NSLS‐II, covers a 5–30 keV photon energy range and delivers a flux of 4.0 × 1012 photons s−1 at 1 Å into a 1 µm × 1.5 µm to 10 µm × 10 µm (V × H) variable focus, expected to reach 5 × 1012 photons s−1 at final storage‐ring current. This flux density surpasses most MX beamlines by nearly two orders of magnitude. The high brightness and microbeam capability of FMX are focused on solving difficult crystallographic challenges. The beamline's flexible design supports a wide range of structure determination methods – serial crystallography on micrometre‐sized crystals, raster optimization of diffraction from inhomogeneous crystals, high‐resolution data collection from large‐unit‐cell crystals, room‐temperature data collection for crystals that are difficult to freeze and for studying conformational dynamics, and fully automated data collection for sample‐screening and ligand‐binding studies. FMX's high dose rate reduces data collection times for applications like serial crystallography to minutes rather than hours. With associated sample lifetimes as short as a few milliseconds, new rapid sample‐delivery methods have been implemented, such as an ultra‐high‐speed high‐precision piezo scanner goniometer [Gao et al. (2018). J. Synchrotron Rad.25, 1362–1370], new microcrystal‐optimized micromesh well sample holders [Guo et al. (2018). IUCrJ, 5, 238–246] and highly viscous media injectors [Weierstall et al. (2014). Nat. Commun.5, 3309]. The new beamline pushes the frontier of synchrotron crystallography and enables users to determine structures from difficult‐to‐crystallize targets like membrane proteins, using previously intractable crystals of a few micrometres in size, and to obtain quality structures from irregular larger crystals. [ABSTRACT FROM AUTHOR]