The largest database of trusted experimental protocols

D max ultima

Manufactured by Rigaku
Sourced in Japan

The D-Max/Ultima is a versatile X-ray diffractometer (XRD) system designed for a wide range of material analysis applications. It provides high-quality data collection and analysis capabilities for phase identification, structural characterization, and quantitative analysis of various solid materials.

Automatically generated - may contain errors

4 protocols using d max ultima

1

Hydroxyapatite Crystallinity Analysis by XRD

Check if the same lab product or an alternative is used in the 5 most similar protocols
The crystallinity of Hydroxyapatite calcinated powders was evaluated by X-ray diffraction (XRD). XRD analysis was performed on calcined powders using a D-Max/Ultima diffractometer (Rigaku, Tokyo, Japan). The particles crystallite size (D) was calculated from the Scherrer equation applied to the diffractogram (Sanosh et al., 2009 (link)):
where λ is the wavelength (Cu Kα), β is the full width at the half-maximum of the HA (2 1 1) line and θ is the diffraction angle. The percentage of secondary phases in HA-Mg powder was evaluated according to the following equation (Sanosh et al., 2009 (link)):
were I1 and I2 represent the intensity of highest peaks present in secondary phases while IHA is the intensity of the highest peak of HA.
+ Open protocol
+ Expand
2

Comprehensive Characterization of Synthesized Products

Check if the same lab product or an alternative is used in the 5 most similar protocols
The micro-structural properties and morphologies of the synthesized products were observed by X-ray diffraction (XRD, D/MAX-Ultima, Cu Kα source, 2° min−1 scanning rate and the scanning angle from 10° to 80° as well as the power was 40 kV and 40 mA, Rigaku, Tokyo, Japan), scanning electron microscopy (SEM, ZEISS Gemini 500, Carl Zeiss AG, Oberkochen, Germany), transmission electron microscopy (TEM, JEM-3200FS, JEOL, Tokyo, Japan), high-resolution transmission electron microscopy (HRTEM, JEM-2100F, JEOL, Tokyo, Japan). Besides, X-ray photoelectron spectroscopy and Brunauer–Emmett–Teller analysis were carried out using XPS, ESCALAB 250XI, Thermo Fisher Scientific, Waltham, MA, USA and BET, ASAP2010C instrument, Norcross GA, USA, respectively.
+ Open protocol
+ Expand
3

Comprehensive Particle Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
The surface topography of the abrasive particles was characterized by using a scanning electron microscope (SEM, FEI Quanta 200F) and the internal structure of the abrasive particles was characterized using a transmission electron microscope (TEM, HITACHI HT7700). Moreover, an X-ray diffractometer (XRD, Rigaku Dmax Ultima+, Japan) was utilized with Cu Kα radiation (λ = 1.5418 Å) within the 2θ range of 10–80°. X-ray photoelectron spectroscopy (XPS, Thermo Scientific K-Alpha, America) was employed for qualitative analysis of the synthesized particle elements.
+ Open protocol
+ Expand
4

Soybean Residue Crystallinity Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
The method of crystallinity determination was slightly modified from Ma et al. [42 (link)]. The XRD curves of the soybean residue samples were obtained using an X-diffractometer (D/Max-Ultima +, Rigaku Corporation, Tokyo, Japanese) with the following parameters: an operating voltage and current of 30 kV and 20 mA, respectively, with a range of 5–90° and a step size of 0.02°. The X-ray source was Cu, and relative crystallinity was calculated by Jade 6.5.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!