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Kryoflex

Manufactured by Bruker
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The KRYOFLEX is a cryogenic cooling device designed for laboratory applications. It provides controlled cooling of samples or components to cryogenic temperatures, typically below 100 Kelvin. The core function of the KRYOFLEX is to enable precise temperature regulation and maintenance of cryogenic conditions for experimental or analytical purposes.

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Lab products found in correlation

Kappa apex 2, by Bruker (1 mentions) Apex2, by Bruker (1 mentions)

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KRYOFLEX low temperature device (2 citations)

2 protocols using kryoflex

1

Crystallization of p-Iodo-Phenylalanine

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The p-iodo-phenylalanine was suspended in water at RT and kept in an open vial under a hood. After 6 months, colourless crystalline needles appeared. Suitable crystals for XRD measurements were analysed without further manipulation. The crystals were measured using Mo-Kα radiation on a Bruker KAPPA APEX II diffractometer with a Bruker KRYOFLEX low temperature device. The crystal structure was solved by direct method and refined against F2 using SHELXL9746 (link). Packing diagrams were generated using Mercury47 . The non-hydrogen atoms were refined anisotropically and hydrogen atoms were fixed geometrically and refined isotropically (CCDC deposition number: 1049844).
Bertolani A., Pirrie L., Stefan L., Houbenov N., Haataja J.S., Catalano L., Terraneo G., Giancane G., Valli L., Milani R., Ikkala O., Resnati G, & Metrangolo P. (2015). Supramolecular amplification of amyloid self-assembly by iodination. Nature Communications, 6, 7574.
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2

Structure Determination of DFNK Crystals

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Crystals of DFNK(para‐iodophenylalanine) were extremely thin, curved yellow sheets or laminae. X‐ray diffraction data were collected from DFNK(para‐iodophenylalanine) crystals with a Bruker APEX‐II diffractometer equipped with microfocus and CCD detector by using MoKα radiation (λ=0.71073 Å) and with a collection of 600“/frame. The crystal was cryo‐cooled (103 K) for data collection (Bruker KRYOFLEX). The structure was solved by SIR200269 and refinements were carried out by full‐matrix least‐squares on F2 using the SHELXL70 program. See the Supporting Information for more detail.
Bertolani A., Pizzi A., Pirrie L., Gazzera L., Morra G., Meli M., Colombo G., Genoni A., Cavallo G., Terraneo G, & Metrangolo P. (2016). Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. Chemistry (Weinheim an Der Bergstrasse, Germany), 23(9), 2051-2058.
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