Since its inception in 1951, Rigaku has been at the forefront of analytical and industrial instrumentation technology. Today, with hundreds of major innovations to their credit, the Rigaku Group of Companies are world leaders in the fields of protein and small molecule X-ray crystallography, general X-ray diffraction (XRD and PXRD), X-ray spectrometry (EDXRF and WDXRF), X-ray optics, semiconductor metrology, Raman spectroscopy, laser induced breakdown (LIBS) spectrometry, automation, computed tomography, nondestructive testing, and thermal analysis.
Cement, petroleum, mining, refining, pulp and paper, wood treating, chemicals, pharmaceuticals, biotechnology, forensics, homeland security, defense, aerospace, energy, metals and alloys, life sciences, polymers and plastics, inks and dyes, cosmetics, nanomaterials, photovoltaics, semiconductors, chemistry, geology and minerals, physics, teaching, and academy.
Based in Tokyo, Japan, Rigaku is a global organization with offices, laboratories, and production facilities around the world. Major production facilities are located in Auburn Hills, Michigan; Austin, Texas; Boston, Massachusetts; Carlsbad, California; Osaka, Japan; Prague, Czech Republic; Tokyo, Japan; Wroclaw Poland ;Tucson, Arizona; The Woodlands, Texas; and Yamanashi, Japan.
Rigaku Corporation
4-14-4, Sendagaya
Tokyo 151-0051, Japan
TELEPHONE
+1(281) 362-2300
FAX
+1(281) 364-3628
E-MAILinfo@rigaku.com
WEB SITEwww.rigaku.com
NUMBER OF EMPLOYEES
Worldwide: 1400
YEAR FOUNDED
1951
Best of the Week: EAS Conference Coverage, IR Spectroscopy, Microplastics
November 22nd 2024Top articles published this week include highlights from the Eastern Analytical Symposium, a news article about the infrared (IR) spectroscopy market, and a couple of news articles recapping spectroscopic analysis of microplastics.
FT-IR Analysis of pH and Xylitol Driven Conformational Changes of Ovalbumin–Amide VI Band Study
November 21st 2024This study uses Fourier transform infrared (FT-IR) spectroscopy to analyze how the globular protein ovalbumin's secondary structures transition under varying pH conditions in the presence of the cosolvent xylitol, highlighting the role of noncovalent interactions in these conformational changes.