Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin

Abstract

Three macromolecular crystallography (MX) beamlines at the HelmholtzZentrum Berlin (HZB) are available for the regional, national and international structural biology user community. The state-of-the-art synchrotron beamlines for MX BL14.1, BL14.2 and BL14.3 are located within the low-section of the BESSY II electron storage ring. All beamlines are fed from a superconducting 7 T wavelength-shifter insertion device. BL14.1 and BL14.2 are energy tunable in the range 5-16 keV, while BL14.3 is a fixed-energy side station operated at 13.8 keV. All three beamlines are equipped with CCD detectors. BL14.1 and BL14.2 are in regular user operation providing about 200 beam days per year and about 600 user shifts to approximately 50 research groups across Europe. BL14.3 has initially been used as a test facility and was brought into regular user mode operation during the year 2010. BL14.1 has recently been upgraded with a microdiffractometer including a mini-goniometer and an automated sample changer. Additional user facilities include office space adjacent to the beamlines, a sample preparation laboratory, a biology laboratory (safety level 1) and highend computing resources. In this article the instrumentation of the beamlines is described, and a summary of the experimental possibilities of the beamlines and the provided ancillary equipment for the user community is given.

Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L

“…a part of the physiological substrate histone H3 and human cathepsin L by crystallizing the complex with a catalytic mutant of the enzyme and elucidating its structure [16]. Refinement confirmed the positioning of only three amino acids from the histone H3 [19][20][21][22][23][24][25][26][27][28][29][30][31][32][33] peptide. Our crystal packing analysis suggested that there is not enough space to accommodate all 14 peptide residues in the available space in the active site cleft.…”

Roquin binding to target mRNAs involves a winged helix-turn-helix motif

“…Data collection, structure determination and refinement. Diffraction data were collected on BL14.1 operated by the Helmholtz-Zentrum Berlin (HZB) at the BESSY II electron storage ring (Berlin-Adlershof, Germany) 23 at wavelengths of 1.0727 or 0.9184 Å, respectively. Data were processed with the program XDSAPP 24 .…”

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

“…and M.G., manuscript in preparation) were soaked in cryosolution containing 10 mM magnesium chloride or 50 mM zinc chloride, respectively, for 1 h before freezing. Diffraction data sets were collected at the MX beamline BL14.1 at the BESSY II electron storage ring (Berlin-Adlershof, Germany) operated by the Helmholtz-Zentrum Berlin 43 , with a MX-225 CCD detector (Rayonix, Evanston, USA). Data sets were collected at 100 K and a wavelength of 0.918 Å (crystal form 1 and 2) or 1.283 Å (Zn-soak) over 200°(crystal form 1, Zn-soak) or 130°(crystal form 2) with 1°(crystal form 1 and 2) or 0.5°(Zn-soak) rotation per frame.…”