Good quality orange-red crystals of Zwitterionic Spirocyclic Meisenheimer complex 1 was obtained from their respective ethyl acetate-dichloromethane solution by slow evaporation. Crystallographic data of compound 1 : C32H47N7O7, Mw = 641.77, monoclinic, space group P21/n, a = 10.9266(6), b = 26.6855(13), c = 11.9495(5) Å, α = 90°, β = 11.858(6)°, γ = 90°, V = 3233.8(3) Å3, Z = 4, dm = 1.318 Mgm−3, T = 293 K, R1 0.0552 and wR2 0.1348 for 7126 data with I > 2σ(I). Intensity data were collected with MoKα radiation using Bruker APEX-2 CCD diffractometer. Data were processed using the Bruker SAINT package and the structure solution and refinement procedures were performed using SHELX97. The non-hydrogen atoms were refined with anisotropic thermal parameters. The data for compound 1 has been deposited at the Cambridge Crystallographic Data Centre with reference number CCDC 1481699.
Apex 2 ccd diffractometer
Manufactured by Bruker
Sourced in Germany, United States
The APEX-II CCD diffractometer is a X-ray single crystal diffraction instrument designed for the determination of crystal structures. It features a charge-coupled device (CCD) detector for efficient data collection. The core function of the APEX-II CCD diffractometer is to collect X-ray diffraction data from single crystal samples and provide the necessary information for the structural analysis of crystalline materials.
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Lab products found in correlation
Saint package, by Bruker (3 mentions)
Sadabs, by Bruker (3 mentions)
Av 500 nmr spectrometer, by Bruker (3 mentions)
Equinox 55 fourier transform infrared spectrometer, by Bruker (3 mentions)
Mz 75 microscope, by Leica (3 mentions)
D8 goniometer, by Bruker (3 mentions)
Sadabs 2016 2, by Bruker (3 mentions)
Tg dsc sta 499 f3 instrument, by Netzsch (2 mentions)
Vario el cube elemental analyzer, by Elementar (2 mentions)
Saint software, by Bruker (2 mentions)
Apex2 program, by Bruker (2 mentions)
Spectrum bx 2, by PerkinElmer (2 mentions)
Digital melting point apparatus 5a 6797, by Gallenkamp (2 mentions)
Synapt g2 mass spectrometer, by Bruker (2 mentions)
Flash 2000 chns o analyzer, by Thermo Fisher Scientific (2 mentions)
377 ft ir spectrometer, by PerkinElmer (2 mentions)
D8 venture diffractometer, by Bruker (2 mentions)
Agilent 6210 tof lc ms spectrometer, by Agilent Technologies (2 mentions)
400 mhz nmr spectrometer, by Bruker (2 mentions)
Xtalab pro diffractometer, by Rigaku (1 mentions)
155 protocols using apex 2 ccd diffractometer
1
Structural Characterization of Zwitterionic Spirocyclic Meisenheimer Complex
2
Single Crystal X-ray Diffraction of ARI Compounds
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ARI2-RSV1·MeOH and ARI-KAE·IPA Single Crystal X-ray Diffraction (SCXRD) data were collected on a Bruker Apex2 CCD diffractometer (graphite monochromated MoKα radiation, λ = 0.71073 Å) (Karlsruhe, Germany) at 296 K. ARI-KAE·EtOH SCXRD data was recorded on XtaLAB PRO diffractometer (graphite monochromated CuKα radiation, λ = 0.154184 Å) (Rigaku, Japan) at 100 K. Data reduction and unit cell refinement were performed with the software SAINT. Crystal structures were solved using direct methods in Shelxs-13 and refined using Shelxl-97 [52 (link)]. All non-hydrogen atoms were refined by using full-matrix least squares methods. CIF files can be obtained free of charge from https://www.ccdc.cam.ac.uk/structures (accessed on 24 March 2021) and the Cambridge Crystallographic Data Centre, Cambridge, UK, with the deposition Number 2072710 (ARI2-RSV1·MeOH), 2072711 (ARI-KAE·EtOH), 2072712 (ARI-KAE·IPA).
3
Crystallographic Analysis of Ligand L
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Crystallographic data for ligand L were collected on a Bruker APEX 2 CCD diffractometer with graphite-monochromated Mo Kα radiation (λ = 0.71073 Å) in the ω scan mode [21 (link)]. The structure was solved by a charge flipping algorithm and refined by full-matrix least-squares methods on F2 [22 (link)]. All esds were estimated using the full covariance matrix. Further details are presented in Table S1 . CCDC: 2059923, L . These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via www.ccdc.cam.ac.uk/data_request/cif (31 January 2021).
4
Crystallographic data collection and analysis
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Crystallographic data for ligand W were collected on a Bruker APEX 2 CCD diffractometer with graphite-monochromated Mo Kα radiation (λ = 0.71073 Å) in the ω scan mode (Krause et al., 2015 (link)). The structure was solved by a charge flipping algorithm and refined by full-matrix least-squares methods on F2 (Sheldrick, 2015 (link)). All esds were estimated using the full covariance matrix. Further details are presented in Supplementary Table S1 .
5
Structural Analysis of Nickel(II) Complex
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The crystal structure analysis of bis{(2-methoxy-6-[(E)-(propylimino)methyl]phenolato}nickel(II) was done by using Bruker APEX 2 CCD diffractometer equipped with ω and φ scan mode with Mo Kα (λ = 0.71073 Å) at T = 298(2) K. The Crystal structure was solved by SHELXL 2014/7 using the direct method and the refinement was performed by full matrix least squares of F2 [38 ]. SAINT and SADABS programs were used to correct the data for Lorentzian, polarisation and absorption effects. EURO VECTOR EA 3000 was used for elemental analysis. Nicolet iS10-FTIR spectrometer was used for IR analysis in the range of 4000 - 450 cm−1. NMR and mass spectral data were acquired by using Bruker Avance III 500 spectrometer and JMS-T100LC Accu ToF respectively. Thermal analysis was carried out using a Hitachi (model 7200) TG/DTA by passing a purge gas of high pure inert N2 of 200 ml/min at a heating rate of 10 °C/min.
6
Single Crystal X-ray Diffraction Analysis
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Orange single crystals (plate-like with 0.952 × 0.685 × 0.264 mm3 for L2) was served for analysis. The samples were set on top of a glass capillary, coated with a thin layer of Araldite epoxy resin. Intensity data were collected on a Bruker APEX2 CCD diffractometer (Bruker, Billerica, MA, USA) with Mo-Kα radiation monochromated by graphite (λ = 0.71073 Å) at 173.2 K. Data treatment used the program package SAINT (Bruker, Billerica, MA, USA). An empirical absorption correction for intensity was applied by the program SADABS (Bruker, Billerica, MA, USA). In this program package, the structures (phase problem) were initially solved by direct methods with a SHELXS-97,22 (link) expanded by Fourier techniques, and finally refined by full-matrix least-squares methods based on F2 using a SHELXL-97 program.22 (link) All non-hydrogen (heavy) atoms were readily located to construct a model and were refined by anisotropic (thermal) displacement parameters. Hydrogen atoms were located at geometrically calculated positions and refined using riding models.36 (link)
7
Crystallization and Structure Determination of Peptides
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Diffraction-quality crystals
of peptides1–3 were obtained from solution by
slow evaporation. Intensity data were collected with Mo Kα (peptide1 and 2 ) or Cu Kα (peptide 3 ) radiation by a Bruker APEX-2 CCD diffractometer. The data were
processed using Bruker SAINT package. The structure solution and refinement
were performed by SHELX97. Refinement of nonhydrogen atoms was performed
using anisotropic thermal parameters. CCDC 197545, 1960546, and 1960544
contain the crystallographic data for the peptides1–3, respectively.
of peptides
slow evaporation. Intensity data were collected with Mo Kα (peptide
processed using Bruker SAINT package. The structure solution and refinement
were performed by SHELX97. Refinement of nonhydrogen atoms was performed
using anisotropic thermal parameters. CCDC 197545, 1960546, and 1960544
contain the crystallographic data for the peptides
8
Structural Elucidation of Peptide Crystals
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Single and transparent
crystals of peptides1–3 had been obtained from
different solutions through solvent evaporation. A Bruker APEX-2 CCD
diffractometer was used to measure the data with MoKα (peptide2 ) or CuKα (peptides 1 and 3 ) radiation. A Bruker SAINT package was used to analyze the data.
SHELX97 was used for solving and refinement of the structure. Nonhydrogen
atoms were refined by anisotropic thermal parameters. The data for
the crystals of peptides1 –3 are
reported in CCDC 2080597 (1), 2080595 (2), and 2080601 (3), respectively.
crystals of peptides
different solutions through solvent evaporation. A Bruker APEX-2 CCD
diffractometer was used to measure the data with MoKα (peptide
SHELX97 was used for solving and refinement of the structure. Nonhydrogen
atoms were refined by anisotropic thermal parameters. The data for
the crystals of peptides
reported in CCDC 2080597 (1), 2080595 (2), and 2080601 (3), respectively.
9
X-ray Crystallographic Analysis of Tripeptides
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Intensity data
of all the reported peptides were collected with MoKα radiation
using Bruker APEX-2 CCD diffractometer. Data were processed using
the Bruker SAINT package and the structure solution and refinement
procedures were performed using SHELX97. Single crystal X-ray analysis
of tripeptides1 and 2 were recorded on
a Bruker high resolution X-ray diffractometer instruments with MoKα
radiation. Data were processed using the Bruker SAINT package and
the structure solution and refinement procedures were performed using
SHELX97. Crystal data: Tripeptide1 : C32H36N4O6, 2(C2H6OS) Mw = 728.90, P na 21, a = 23.8893(6) Å, b = 10.0574(2) Å, c = 30.8929(7) Å, α = 90° β = 90°,
γ = 90°, V = 7422.5(3) Å3, Z = 8, dm = 1.305
Mg m–3, T = 100 K, R1 = 0.0614 and wR2 = 0.1565 for 12903 data with I > 2σ(I). Tripeptide2 : 2(C31H34N4O8, 2(C7H8), Mw = 682.76, P1, a = 11.4783(2) Å, b = 11.9570(5) Å, c = 15.2501(9) Å, V = 1824.3(2) Å3, Z = 2, dm = 1.243 Mg m–3, T = 100, R1 = 0.0519 and wR2 = 0.1341 for 8780 data with I > 2σ(I). CCDC: 2090664 and 2090665 contains the supplementary
crystallographic data for foldamer1 and 2 .
of all the reported peptides were collected with MoKα radiation
using Bruker APEX-2 CCD diffractometer. Data were processed using
the Bruker SAINT package and the structure solution and refinement
procedures were performed using SHELX97. Single crystal X-ray analysis
of tripeptides
a Bruker high resolution X-ray diffractometer instruments with MoKα
radiation. Data were processed using the Bruker SAINT package and
the structure solution and refinement procedures were performed using
SHELX97. Crystal data: Tripeptide
γ = 90°, V = 7422.5(3) Å3, Z = 8, dm = 1.305
Mg m–3, T = 100 K, R1 = 0.0614 and wR2 = 0.1565 for 12903 data with I > 2σ(I). Tripeptide
crystallographic data for foldamer
10
Single Crystal X-ray Diffraction of Streptomyces cuboideum
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Diffraction intensities for single S. cuboideum crystals (orange and red) were collected at 173 K on a Bruker Apex2 CCD diffractometer (Bruker, Portland, OR, USA) using an Incoatec Cu IµS source, Cu Kα radiation, 1.54178 Å. The space group was determined based on systematic absences. Absorption correction was applied by SADABS [25 ]. Structures were solved by direct methods and Fourier techniques and refined on F2 using full matrix least-squares procedures. All non-H atoms were refined with anisotropic thermal parameters. H atoms were found on the residual density map and refined with isotropic thermal parameters. All calculations were performed by the Bruker SHELXL-2014/7 packages [26 (link)] (Bruker, Portland, OR, USA).
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