Diffractograms of F1–F4 were developed using a powder X-ray diffractometer (Rigaku RU200, Rigaku Corp., Tokyo, Japan). The measuring conditions were as follows: graphite-monochromated Cu Kα radiation; voltage 40 kV, 300 mA and angle speed of 4 °C/min over the range of 5–45°.
Ru200
Manufactured by Rigaku
Sourced in Japan
The RU200 is a compact and versatile X-ray diffractometer designed for laboratory use. It is capable of performing a wide range of X-ray diffraction analysis techniques, including powder diffraction, thin-film analysis, and single-crystal diffraction. The RU200 incorporates a sealed X-ray tube and a high-performance detector to provide accurate and reliable data, making it a valuable tool for materials research, quality control, and other applications requiring X-ray diffraction analysis.
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10 protocols using ru200
1
X-Ray Diffraction Analysis of F1-F4
2
Structural Determination of Pct1 Protein
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Aliquots of a mixture of 140 µM Pct1, 2 mM tripolyphosphate, 5 mM manganese chloride were mixed on a cover slip with an equal volume of precipitant solution containing 2.8 M sodium chloride, 10% (w/v) PEG6000. Crystals were grown at 18°C by hanging drop vapor diffusion against the precipitant solution, then flash-frozen in liquid nitrogen. Diffraction data from a single crystal to 2.6 Å resolution were collected on a Rigaku RAXIS-4 image plate detector with CuKα radiation from a Rigaku RU200 rotating anode generator. The data were indexed, integrated and scaled using HKL2000 (Otwinowski and Minor 1997 ). The crystal was in space group P21. Initial phases were obtained by molecular replacement in PHASER (McCoy et al. 2007 (link)) using the coordinates of the S. cerevisiae Cet1 homodimer (pdb 1D8I) as the search model. Iterative rounds of refinement and adjustment in CNS (Brunger et al. 1998 (link)), PHENIX (Adams et al. 2010 (link)), and COOT (Emsley and Cowtan 2004 (link)) yielded a 2.6 Å Pct1 model with R/Rfree of 0.199/0.245 and good geometry (97.9%, 99.9%, and 0.1% in favored, allowed, and disallowed regions of Ramachandran space, respectively) (Chen et al. 2010 (link)). The model contained four Pct1 protomers in the asymmetric unit organized as two homodimers (A/B and C/D). No electron density was observed for tripolyphosphate or manganese.
3
Crystallization and Structure Determination of FnLpxA
4
Comprehensive Characterization of Mg-HAP Nanoparticles
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Phase compositions and crystal sizes of the nanocrystals were characterized by XRD (Rigaku RU-200). Surface charges of HAP and Mg-HAP nanocrystals in deionized water were determined by dynamic light scattering using a Zetasizer Nano Series. Surface morphologies of the nanoparticles were observed by TEM (JEOL JEM-2100) with SAED. Functional groups of HAP and Mg-HAP nanoparticles were analyzed by FTIR (Nicolet Nexus 670). Chemical compositions of the nanoparticles were quantified by EDS (QUANTAX 400-30).
5
X-ray Fluorescence Characterization Protocol
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X-ray fluorescence (XRF) experiments were carried out with Molybdenum rotating anode X-ray generator (Rigaku RU200) coupled with multilayer W/Si optics (Xenocs) delivering a focalized and monochromated (λ = 0.711 Å) X-ray beam of 150 × 150 μm. Fluorescence spectra were measured with an energy-dispersive detector (SDD detector, Ketek), with a time acquisition of 240 min. XRF analysis was performed with PyMca software (Solé et al., 2007 (link)).
6
X-ray Crystallographic Structure Determination
7
Cryoprotection and X-ray Diffraction of Protein Crystals
8
Structural Determination of INPP1 Crystals
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INPP1 diffraction data from capillary mounted crystals were collected on dual Xuong-Hamlin Mark II multiwire area detectors (39 (link)) equipped with helium boxes using CuKα X-rays generated by a Rigaku RU200 rotating anode. As was the case with the original INPP1 data sets (11 (link)), several data sets had to be reindexed from h,k,l to h, -k, -l to keep indexing consistent. This problem arises from the physical orientation along the C axis of crystals with P4 point groups. Inverse beam experiments were used to collect anomalous data by complementing ϕ,χ orientations with ϕ + 180°, -χ orientations. Data were reduced, merged, and scaled using the area detector software (40 (link)). Data from the inverse beam experiments were reduced without merging the Bijvoet pairs and were subsequently used to calculate the anomalous signal component. In preparation for structure solution and refinement, reflection files were converted to mtz format and assigned a conserved Rfree set using the program f2mtz (41 ).
INPP1D54A and substrate complex diffraction data were collected on an R-Axis IIc image plate detector using monochromatic Cu Kα X-rays (λ = 1.5418 Å) at 4 °C to prevent crystal decay and were processed using DENZO and SCALEPACK (42 ).
INPP1D54A and substrate complex diffraction data were collected on an R-Axis IIc image plate detector using monochromatic Cu Kα X-rays (λ = 1.5418 Å) at 4 °C to prevent crystal decay and were processed using DENZO and SCALEPACK (42 ).
9
Structural Insights into Oligopeptidase B
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All diffraction data were collected at 100 K. A data set was collected from crystal 1 on a home diffractometer (Rigaku RU200 generator, blue optics, R-AXIS IV ++ detector; wavelength 1.5418 A ˚, ' range of 100.5 with an increment of 0.5 ; crystal-to-detector distance 100.03 mm). The data set from , 1998 , 2001; Szeltner, Rea, Juha ´sz et al., 2002; Szeltner, Rea, Renner et al., 2002; Shan et al., 2005; Li et al., 2010 ), oligopeptidase B (McLuskey et al., 2010; Canning et al., 2013) , puromycin hydrolase (Matoba et al., 2011) and AAP from A. pernix (Bartlam et al., 2004; Kiss et al., 2007 Kiss et al., , 2008;; Harmat et al., 2011) . The catalytic triad is only accessible through the propeller channel. (b) A monomer with a permanent side entrance as found in DPP-IV (for examples, see Rasmussen et al., 2003; Engel et al., 2003; Thoma et al., 2003; Nordhoff et al., 2006; Nakajima et al., 2008) , tripeptidyl aminopeptidase (Ito et al., 2006)
10
Elemental Composition Analysis via XRF
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X-ray fluorescence allows precise determination of the elemental composition of the sample. Experiments were carried out with a molybdenum rotating anode X-ray generator (RIGAKU RU200) coupled with multilayer W/Si optics delivering a focalized and monochromated (λ=0.711 Å) X-ray beam of 150 µm x 150 µm size.
Fluorescence spectra were measured with an energy dispersive detector (SDD detector @Ketek), with a time acquisition of 1500 s each. XRF analysis was performed with PyMca software (22) .
Fluorescence spectra were measured with an energy dispersive detector (SDD detector @Ketek), with a time acquisition of 1500 s each. XRF analysis was performed with PyMca software (22) .
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