Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin - PubMed (original) (raw)

Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin

Uwe Mueller et al. J Synchrotron Radiat. 2012 May.

Abstract

Three macromolecular crystallography (MX) beamlines at the Helmholtz-Zentrum 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-β 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-κ 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 high-end 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.

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Figures

Figure 1

Figure 1

The 7T-WLS installed in the low-β section 14 of the BESSY II storage ring.

Figure 2

Figure 2

Photon flux of beamlines BL14.1, BL14.2 and BL14.3 as a function of energy.

Figure 3

Figure 3

Upstream view of the joint optics hutch. BL14.2 and BL14.3 comprise the left part of the image, BL14.1 the right. The open green sliding door on the right-hand side is the only access to the optics hutch.

Figure 4

Figure 4

Schematics of the beamline layout for beamlines BL14.1, BL14.2 and BL14.3. The three beamlines are horizontally separated by the usage of the 40 mrad broad synchrotron beam fan. The BESSY storage ring wall is located at the downstream side of the primary beam-shutter.

Figure 5

Figure 5

Experimental stations instrumentations: (a) BL14.1, (b) BL14.2, (c) BL14.3.

Figure 6

Figure 6

Three-dimensional drawing of the MX beamline optics (left) and experimental hutches (centre) as well as the experiment control room and sample preparation laboratory (upper right). Beamline order from top to bottom: BL14.1, BL14.2, BL14.3.

Figure 7

Figure 7

Ancillary facilities of the MX beamlines. (a) UV-RIP set-up on BL14.1. The crystal which is exposed to UV irradiation can easily be seen owing to its fluorescence, (b) In situ crystal screening of 96-well plates centred within the X-ray beam of BL14.1. (c) Noble gas pressure cell for Xe and Kr derivatizations (

http://www.hamptonresearch.com/

). (d) HC1c dehydration device mounted on BL14.3. (e) Cryo-shutter annealing device at BL14, with microdiffractometer MD2 and mini-κ MK3. (f) Results from the cryo-shutter operation (the device mounted on all beamlines); the image shows a diffraction pattern before (left) and after (right) cryo-annealing.

Figure 8

Figure 8

Histogram of released protein structure coordinates per year from the PDB (data were taken from the BioSync web page,

http://biosync.sbkb.org/

). As a consequence of the 12-months hold on deposited structures, the deposition numbers for 2011 will only be finalized by the end of 2012. Status from 9 February 2012.

Figure 9

Figure 9

Representative examples of research highlights from diffraction data collected at the HZB MX beamlines. (a) Meta II rhodopsin structure (Choe et al., 2011 ▶), (b) 66.3 kDa protein structure solved by S-SAD (Lakomek et al., 2009 ▶), (c) α1-acid glycoprotein solved by UV-RIP with highlighted disulfide bonds and contoured +4.5σ and −4.5σ (green and red, respectively) F before − F after difference density (Schönfeld et al., 2008 ▶).

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