Development of an in-vacuum x-ray microscope with cryogenic sample cooling for beamline P11 at PETRA III

Meents, A.; Reime, B.; Stuebe, Nicolas; Fischer, P.; Warmer, Martin; Goeries, Dennis; Roever, Jan; Meyer, Jan; Fischer, Janine; Burkhardt, Anja; Vartiainen, Ismo; Karvinen, Petri; Dávid, Christian

doi:10.1117/12.2027303

Cited by 30 publications

(23 citation statements)

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“…The characteristics of the three MX beamlines at PETRA III are summarized in Table 1. 2.2. Beamline P11 @ DESY DESY beamline P11 provides two state-of-the-art endstations for structural investigations of biological samples at different length scales: an X-ray microscope with a resolution of up to 10 nm [9,10,11] and a crystallography experiment. The crystallography endstation (shown in Figure 2) is operated between 5.5 keV and 30 keV and provides full SAD/MAD capability.…”

Section: 1overviewmentioning

confidence: 99%

Status of the crystallography beamlines at PETRA III

et al. 2016

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Since 2013, three beamlines for macromolecular crystallography are available to users at the thirdgeneration synchrotron PETRA III in Hamburg: P11, P13 and P14, the latter two operated by EMBL. Beamline P11 is operated by DESY and is equipped with a Pilatus 6M detector. Together with the photon flux of 2 × 10 13 ph/s provided by the very brilliant X-ray source of PETRA III, a full data set can be typically collected in less than 2 min. P11 provides state-of-the-art microfocusing capabilities with beam sizes down to 1 × 1 µm 2 , which makes the beamline ideally suited for investigation of microcrystals and serial crystallography experiments. An automatic sample changer allows fast sample exchange in less than 20 s, which enables high-throughput crystallography and fast crystal screening. For sample preparation, an S2 biosafety laboratory is available in close proximity to the beamline.

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Section: 1overviewmentioning

confidence: 99%

Status of the crystallography beamlines at PETRA III

et al. 2016

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“…CuTCNPP is situated on a crystallographic centre of symmetry and exhibits an r.m.s. deviation from exact molecular C 2h point group symmetry of 0.047 Å , as calculated with MOLSYM in PLATON (Spek, 2009 Computer programs: P11 Crystallography Control (Meents et al, 2013), XDS (Kabsch, 2010), SUPERFLIP (Palatinus & Chapuis, 2007), EDMA (Palatinus et al, 2012), SHELXL2014 (Sheldrick, 2015), DIAMOND (Brandenburg, 2014) and enCIFer (Allen et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

A synchrotron study of [5,10,15,20-tetrakis(3-cyanophenyl)porphyrinato-κ⁴N⁵,N¹⁰,N¹⁵,N²⁰]copper(II) nitrobenzene trisolvate at 80 K

et al. 2016

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Porphyrin assemblies display interesting photophysical properties and a relatively high thermal stability. Moreover, meso-functionalized porphyrins with virtually fourfold symmetry can be relatively readily synthesized from pyrrole and the appropriate aldehyde. A number of metallo derivatives of 5,10,15,20-tetrakis(4-cyanophenyl)porphyrin, where the N atom of the linear cyano group can act both as a donor for coordination bonds or as an acceptor for hydrogen bonds, have been structurally characterized by single-crystal X-ray analysis. The supramolecular and structural chemistry of the corresponding 2- and 3-cyanophenyl isomers of the parent porphyrin, however, has remained largely unexplored. The crystal structure of [5,10,15,20-tetrakis(3-cyanophenyl)porphyrinato]copper(II) (CuTCNPP) nitrobenzene trisolvate, [Cu(CHN)]·3CHNO, has been determined at 80 K by synchrotron single-crystal X-ray diffraction. CuTCNPP exhibits a C-symmetric ααββ conformation, despite an unsymmetrical crystal environment, and is situated on a crystallographic centre of symmetry. The Cu ion adopts a genuine square-planar coordination by the four pyrrole N atoms. The 24-membered porphyrin ring system shows no marked deviation from planarity. In the crystal, the CuTCNPP molecules and two nitrobenzene molecules are face-to-face stacked in an alternating fashion, resulting in corrugated layers. The remaining nitrobenzene guest molecule per CuTCNPP resides in the region between four neighbouring columnar stacks of CuTCNPP and sandwiched nitrobenzene molecules, and is disordered over four positions about a centre of symmetry.

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“…Collection of X-ray diffraction data, structure determination and refinement X-ray diffraction data were recorded on beamline P11 (Meents et al 2013) of Petra III at the DESY (Hamburg, Germany) and on beamline 14.2 (Mueller et al 2012) of the BESSY II electron storage ring (Berlin-Adlershof, Germany). Integration of X-ray data and space group assignment was carried out with XDS (Kabsch 2010).…”

Section: Crystallizationmentioning

confidence: 99%

The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown

Gumz

Krausze²,

Eisenschmidt

et al. 2015

Plant Mol Biol

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Kelch repeat-containing proteins are involved in diverse cellular processes, but only a small subset of plant kelch proteins has been functionally characterized. Thiocyanate-forming protein (TFP) from field-penny cress, Thlaspi arvense (Brassicaceae), is a representative of specifier proteins, a group of kelch proteins involved in plant specialized metabolism. As components of the glucosinolate-myrosinase system of the Brassicaceae, specifier proteins determine the profile of bioactive products formed when plant tissue is disrupted and glucosinolates are hydrolyzed by myrosinases. Here, we describe the crystal structure of TaTFP at a resolution of 1.4 Å. TaTFP crystallized as homodimer. Each monomer forms a six-blade β-propeller with a wide "top" and a narrower "bottom" opening with distinct strand-connecting loops protruding far beyond the lower propeller surface. Molecular modeling and mutational analysis identified residues for glucosinolate aglucone and Fe(2+) cofactor binding within these loops. As the first experimentally determined structure of a plant kelch protein, the crystal structure of TaTFP not only enables more detailed mechanistic studies on glucosinolate breakdown product formation, but also provides a new basis for research on the diverse roles and mechanisms of other kelch proteins in plants.

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Development of an in-vacuum x-ray microscope with cryogenic sample cooling for beamline P11 at PETRA III

Cited by 30 publications

References 0 publications

Status of the crystallography beamlines at PETRA III

Status of the crystallography beamlines at PETRA III

A synchrotron study of [5,10,15,20-tetrakis(3-cyanophenyl)porphyrinato-κ⁴N⁵,N¹⁰,N¹⁵,N²⁰]copper(II) nitrobenzene trisolvate at 80 K

The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown

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Development of an in-vacuum x-ray microscope with cryogenic sample cooling for beamline P11 at PETRA III

Cited by 30 publications

References 0 publications

Status of the crystallography beamlines at PETRA III

Status of the crystallography beamlines at PETRA III

A synchrotron study of [5,10,15,20-tetrakis(3-cyanophenyl)porphyrinato-κ4N5,N10,N15,N20]copper(II) nitrobenzene trisolvate at 80 K

The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown

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A synchrotron study of [5,10,15,20-tetrakis(3-cyanophenyl)porphyrinato-κ⁴N⁵,N¹⁰,N¹⁵,N²⁰]copper(II) nitrobenzene trisolvate at 80 K