Overview
Beam line 12-1 employs a 154-pole, 1-Tesla in-vacuum undulator, a flat side-deflecting Rh-coated Si mirror, and a liquid nitrogen-cooled double-crystal Si(111) monochromator with a 0.01% energy bandpass. The beamline is also fitted with a multilayer with a ~1% energy bandpass that boosts the x-ray flux by a factor by about two orders of magnitude.. Kirkpatrick-Baez (KB) optical mirrors are used for 18:1 horizontal and 12:1 vertical beam focusing. The vertical mirror polish is ~100 nrad RMS and a vertical beam focus of ~5 µm FWHM.
BL12-1 is a preeminent macromolecular crystallography capability for structural biology research in the US and is designed for investigations of the most challenging structural investigations of biological systems confronting scientists today, including cases where crystals can only be grown to a few microns in size. BL12-1 is competitive with the performance of the best in class micro-beam instruments in the US (e.g., the native vertical focus of 5 µm and a collimated beam size of 1.5 µm2 produces a flux density > 6x that of SSRL BL12-2).
BL12-1 has improved performance at low energy and is equipped with an Eiger 16M pixel array detector with readout speeds over 100 Hz full detector and over 750 Hz for regions of interest which enables ultra-high-redundancy SAD experiments and routine serial crystallography experiments using liquid jets.
BL12-1 is also an effective gateway for the Linac Coherent Light Source (LCLS), providing a similar platform to the LCLS-MFX instrument for equipment R&D, testing, prescreening and characterization of micro- to nano-crystalline samples prior to LCLS studies.
See the Macromolecular Crystallography website for technical details.
Status —
Source —
Instrumentation —
Detector | Dectris EIGER 2XE shutterless data collection, fine phi slicing experiments, serial diffraction |
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Goniometer | Single-axis micro-diffractometer, air bearing, coaxial cold stream, 1.5 micron SOC |
Sample Exchange Robot | Stanford Automated Mounter compatible with magnetic sample bases inside |
Other | SSRL cassettes, Universal Pucks or SSRL in-situ plates |
Stanford Automated Mounter |
Sample Environment —
Sample temperature | 100K - elevated temperatures or room temperature at controlled humidity |
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Other | Cryogenic Temperatures (Oxford Cryo-cooler) |
Elevated Temperature (Oxford Cryo-cooler) | |
Controlled Humidity (Arinax Humidity Control Device) |
Publications
Publications
Highlights
Science Highlights
Beam Line 12-1 Science Highlights
Structural Intermediate of Transglutaminase 2 in Complex with Two Calcium Ions Sheds Light on New Treatments for Celiac Disease
Crystallography Confirms De Novo Protein Binding Modes and Hotspots
How Epstein-Barr Virus Infection Triggers Multiple Sclerosis
First Atomic Structure of an Intact Polyketide Synthase Revealing Two Asynchronous Reaction Chambers
Junctophilin: A Hot Spot for Cardiomyopathy Mutations
Structure of a Small Riboswitch that Binds Two Metabolite Ligands in One Pocket
Structure-based Tuning of Interleukin Receptor Complexes to Promote Anti-tumor Immunity
Evidence for a Dynamic Mo-nitrogenase Metallocofactor during Dinitrogen Reduction
Design of Novel Protein Cages
Shedding Light on Photoisomerization: Electrostatic Control of Excited State Reaction Pathways within Proteins
A Spider Toxin Catches a Sodium Channel Involved in Pain Perception in Action
Structure and Functional Binding Epitopes of V-domain Ig Suppressor of T-Cell Activation (VISTA)
Winning the Fight against Influenza
Structural Basis of Neurosteroid Anesthetic Action on GABAA Receptors
Mechanism of Thiopurine Resistance in Acute Lymphoblastic Leukemia
A Structural Switch that Couples TCR Ligand Binding to Signaling
Revealing the Functional Principles of a Multi-protein Assembly that Uses MicroRNAs
Structural Study of Potent Peptidic Fusion Inhibitors of Influenza Virus Hemagglutinin
Demanding Catalysis via Energy-conserving Electron Bifurcation
Unraveling the Assembly Principles of Bacterial Microcompartments
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