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BL19U1 Protein Complex Crystallography beamline

Scientific goals

The structure of protein complexes is the foundation for elucidating the function of proteins that bind to each other. The structural study of protein complexes has become one of the important frontier fields in structural biology research.The protein complex crystallography beamline is intended to solve the structures of protein or protein complex crystals with large unit cells, such as molecular machines, organelles, viruses, ribosome complexes, etc., with high flux and low divergence.

Techniques and methods

X-ray single crystal diffraction, Single-wavelength anomalous diffraction (SAD), Multi-wavelength anomalous diffraction (MAD), Molecular replacement (MR).

Beamline Layout

 

Beamline specification

Energy range (keV)

7-15

Energy resolution (DE/E)

2×10-4

Wavelength range (？)

0.82-1.77

Focused Beam size (FWHM) (μm2)

120 × 80 (@12keV)

Flux (at 12kev, 300 mA) (photons s-1)

1.5×1012 ph/s

Focused beam divergence (H×V) (mrad2)

￡0.1×0.1

Endstation

Source type

Undulator, U20

Mirrors

1.0 m-long Rh-coated focusing mirror 3.5 mrad

Monochromator

LN2-cooled DCM with Si(111) crystals

Goniometer

MD2 microdiffractometer

Cryo capability

80-400K, LN2 Oxford700 Cryosystem

Sample mounting

Manual/Rigaku Actor automounter

Detector type

CMOS hybrid pixel

Detector model

Pilatus3 6M