Atlas ccd detector

The single crystal X-ray experiments for both compounds were performed at 100 K. The data were collected using a SuperNova kappa diffractometer with Atlas CCD detector (Agilent Technologies, Santa Clara, CA, USA). For the integration of the collected data, the CrysAlis^Pro software (version 1.171.38.41q, 2015; Rigaku Oxford Diffraction, Sevenoaks, UK) was used. The solving and refining procedures were similar for both compounds. The structures were solved using direct methods with the SHELXS97 software, and the solutions were refined using SHELXL-2014/7 program [22 (link)]. CCDC 1573894-1573895 contains supplementary crystallographic data for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via: http://www.ccdc.cam.ac.uk/data_request/cif.

The crystals for analysis were prepared by the slow evaporation method. Single X-ray crystallography was obtained for the crystals using a SuperNova diffractometer (Agilent Technologies, Santa Clara, CA, USA) with an Atlas CCD detector (Agilent Technologies, Santa Clara, CA, USA). The collected data were reduced using the program SAINT, and an empirical absorption correction was carried out using SADABS. The structure was solved by direct methods using Olex2 [24 (link)] and refined by the full-matrix least-squares method using SHELXL [25 (link)]. All non-H atoms were anisotropically refined, while hydrogen atoms were positioned geometrically and refined isotropically. The molecular graphics were made using mercury [26 (link)]. CCDC 154632 and CCDC 2259882 contained the supplementary crystallographic data for this paper. These data can be obtained free of charge via http://www.ccdc.cam.ac.uk/structures/ (accessed on 25 March 2023) (or from the CCDC, 12 Union Road, Cambridge CB2 1EZ, UK; Fax: +44-1223-336033; E-mail: deposit@ccdc.cam.ac.uk).

A 5 μL droplet of each peptide-analogue solution was placed between two aligned siliconized glass rods mounted on a glass slide, spaced approximately 2 mm apart and oriented horizontally, as collinearly as possible. Each sample was allowed to air-dry slowly at ambient temperature and humidity for approximately 30 min to form an oriented fiber suitable for X-ray diffraction. The X-ray diffraction patterns were collected using a SuperNova-Agilent Technologies X-ray generator equipped with a 135-mm ATLAS CCD detector and a 4-circle kappa goniometer (CuKα high-intensity X-ray micro-focus source, λ = 1.5418 Å), operated at 50 kV, 0.8 mA, installed at the Instruct-EL hub, Institute of Chemical Biology, National Hellenic Research Foundation, which is part of the national research infrastructure on structural biology Inspired. The oriented fiber sample was mounted onto the goniometer, and the specimen-to-film distance was set at 52 mm, with an exposure time of 400 s. Each X-ray diffraction pattern was initially viewed using the CrysAlisPro v. 171.40.67a software [24 ] and consequently displayed and measured with the aid of the iMosFLM v. 7.3.0 software [25 (link)].