Measurement of diffraction patterns from protein crystals

The R-AXIS IV++ is arguably the most productive X-ray area detector in the history of macromolecular crystallography. In production for well over a decade and continuously improved during that time period, the success of the R-AXIS IV++ is a testament to the suitability of imaging plate technology for measuring the diffraction patterns from protein crystals.

Engineered for performance

It combines two large active area imaging plates with fast readout speeds and a wide dynamic range, making it ideal for collecting accurate diffraction data from the widest ranges of samples in the home laboratory. High dynamic range is achieved through use of a dual photomultiplier configuration that allows high intensities to be measured by a second, attenuated photomultiplier.

Low cost of ownership

Combining a well-proven, time-tested design with the lack of a need for calibration means that the R-AXIS IV++ is a detector that can be maintained in the field with a minimum of downtime.

The proof is in the results

Structures determined from data measured on the R-AXIS IV++ are well represented in the PDB. In fact, the R-AXIS IV++ has been used to solve more SAD structures in the homelab than any other area detector, without resorting to any special data collection strategies.