This month, we’re spotlighting the XtaLAB Synergy-R. Rigaku Reagents highlights the Berkeley Screen for robust protein crystallization screening. Emilia describes advanced features in GRAL to aid space group determination in challenging cases.
On December 31, 2025, the US National Committee for Crystallography ceases to exist after nearly eight decades of service to the community and representation of the US to the IUCr. The good news is that on January 1, 2026, the American Union of Crystallography will resume the mission of the USNC/Cr and represent the US at the Congress in 2026. The AUC has created the George M. Sheldrick Award for Contributions to Structural Science. The George M. Sheldrick Award for Contributions to Structural Science recognizes outstanding contributions to the field of molecular structure determination, including innovative methods, algorithms, or software. This award celebrates non-tenured and early-career researchers who push the boundaries of molecular structure analysis by creating new tools or refining existing ones to solve complex structural problems. Nominations are open until January 18, 2026.
I want to remind you that we have scheduled a live Rigaku School for Practical Crystallography on basic topics in crystallography from January 26 to February 6, 2026, beginning at 6 AM GMT.
This month, we’re spotlighting the XtaLAB Synergy-R. Rigaku Reagents highlights the Berkeley Screen for robust protein crystallization screening. Emilia describes advanced features in GRAL to aid space group determination in challenging cases.
Be sure to check out the Crystallography in the News section for cutting-edge research. Jeanette reviews Caroline Criado Perez’s Invisible Women: Exposing Data Bias in a World Designed for Men.
Our LinkedIn groupshares information and fosters discussion about X-ray crystallography and SAXS topics. Connect with other research groups and receive updates on how they use these techniques in their own laboratories. You can also catch up on the latest newsletter or Rigaku Journal issue. We also hope that you will share information about your own research and laboratory groups.
Atrigakuxrayforum.comyou can find discussions about software, general crystallography issues and more. It’s also the place to download the latest version of Rigaku Oxford Diffraction’sCrysAlisProsoftware for single crystal data processing.
IUCr2026: A Global Gathering for Structural Science
Join us in Calgary, Alberta, from August 11–18, 2026, for the 27th Congress and General Assembly of the International Union of Crystallography (IUCr2026). This triennial event will welcome over 2,500 scientists, researchers, and students from around the world.
IUCr2026 will feature a dynamic scientific program with symposia, workshops, and satellite meetings spanning crystallography, structural biology, materials science, and beyond. It’s a unique opportunity to connect with the global structural science community, share your research, and spark new collaborations.
Calgary is a vibrant, welcoming city known for its summer festivals, diverse dining, and walkable downtown. It’s also the gateway to breathtaking destinations like Banff and Lake Louise—perfect for pre- or post-congress adventures in the Canadian Rockies.
We will be holding a live Rigaku School for Practical Crystallography on basic topics in crystallography from January 26 - February 6, 2026, beginning at 6 AM GMT and running for up to 90 minutes each day. (Use thisTime Zone converterto determine your local time.)
The majority of the time will be spent on small molecule crystallography. This is a great opportunity for people interested in crystallography who would like to gain a basic foundation of single crystal analysis from a practical point of view.
We hope that you both enjoy and gain something from this School and look forward to meeting you, virtually.
A powerful and fast system for single crystal X-ray diffraction analysis
The XtaLAB Synergy-R was designed to address the increasing need to investigate smaller and smaller samples in crystallographic research. Tightly integrating a PhotonJet-R microfocus rotating anode X-ray source with a high-speed kappa goniometer and a solid-state pixel array HPC detector creates a single crystal diffractometer that produces up to 10 times the flux as compared to a PhotonJet-S microfocus sealed tube source. The increase in flux allows you to look at much smaller crystals than before and as a side benefit it provides increased data collection speed for normal sized crystals.
XtaLAB Synergy-R Overview
The system can be equipped with your choice of HPC hybrid photon counting detectors, theHyPix-6000HEor the curved, large theta coverage detectors,HyPix-Arc 100° or HyPix-Arc 150°. For crystallographers who wish to have a powerful, well-integrated diffractometer and only need to use one port of the rotating anode, the XtaLAB Synergy-R provides the perfect combination of high-flux performance with a low-noise HPC X-ray detector. The XtaLAB Synergy-R now comes equipped with our new UG3 goniometer, which offers faster, more efficient data collections. For more information about the UG3,please see the overview page.
PhotonJet-R
The PhotonJet-R comes from the same pedigree as theMicroMax™-007 HF, of which there are well over 1000 units in use around the world. The PhotonJet-R X-ray source applies the lessons learned over the development and lifetime of the MicroMax-007 rotating anode to produce a new generation, high performance rotating anode source. With the source mounted directly onto the goniometer the XtaLAB Synergy-R provides a stable and robust solution which ensures consistently high performance. Confocal optics, designed by Rigaku Innovative Technologies, offer a high-brilliance X-ray beam and the optional continuously variable slit assembly gives the user the ability to adjust high brilliance versus low divergence depending on the needs of the sample being studied.
Proven reliability
The PhotonJet-R source was designed with reliability in mind. Clever Rigaku engineering makes filament changes easy, like swapping a printer cartridge, with no need to realign the source each time. Scheduled maintenance involves one annual visit from a Rigaku engineer, as with all XtaLAB Synergy diffractometers, and typically takes 1-2 days. With the anode exchange program, you get the benefit of rotating anode power with the convenience of sealed tubes.
Beam conditioning
Where overlapping peaks are a concern, e.g. large unit cells, twins or incommensurate lattices, high beam divergence is undesirable. On the PhotonJet-R source, a software controlled, motorized variable beam slit is available as an option to alter divergence to adapt the source to your sample’s requirements. For those samples where intensity matters most, the slit can be fully opened giving the highest flux. For those where peak sharpness and overlap are factors, the beam can be limited to a divergence anywhere between 1 to 10 mrad.
HyPix detectors
Rigaku’s own HyPix family of HPC detectors use solid state pixel array technology to enable direct X-ray photon detection and counting. Direct X-ray photon detection means that X-ray photons are counted instantaneously as they arrive at the detector. There is no conversion to visible light by a scintillator so the energy of the photon can be assessed at moment of detection. This leads to essentially noise free images. The HyPix detectors feature a 100 Hz frame rate which allows for data fine slicing even at the fastest goniometer speeds. The HyPix detectors incorporate dual counters enabling several modes of operation. Rapid alternating counter electronics (RACE) technology enables the 100 Hz zero dead time mode, ensures that no pixel is blind for more than a few nanoseconds during exposure to X-rays. The high dynamic range mode combines the counters to offer a massive 31-bit counter depth. Dual thresholding offers differential modes and selective signal suppression.
CrysAlisPro
The XtaLAB Synergy-R comes complete withCrysAlisPro, our user-inspired data collection and data processing software for single crystal analysis. Designed around an easy-to-use graphical user interface, CrysAlisPro can be operated under fully automatic, semi-automatic or manual control. CrysAlisPro combines automated crystal screening, the fastest and most accurate strategy software available, concurrent data reduction and automatic small molecule structure solution. CrysAlisPro can operate either in a protein or small molecule dedicated workflow. Popular third-party protein data processing packages can easily process diffraction data if desired. Visual feedback is provided for each step with clear, color-coded guidance so that both novices and experts can collect high-quality data in the shortest time possible.
AutoChem
AutoChem is the ultimate productivity tool for small molecule chemists, offering fast, fully automatic structure solution and refinement during data collection. Developed in collaboration with OlexSys Ltd (Durham University, UK), AutoChem works in conjunction with Olex² where more advanced structure solution and refinement functionality exists. AutoChem is seamlessly integrated within CrysAlisPro, and forms an integral part of our ‘What is this?’ feature. The ‘What is this?’ feature gives you structures quickly and ensures you are not wasting time collecting full datasets on known samples or starting materials. It is an alternative pre-experiment option, which is used to plan your full data collections.
Unlock the next level of macromolecular crystallization with the Berkeley Screen, a rigorously designed 96-condition screen created from deep statistical analysis of the Biological Macromolecular Crystallization Database and decades of crystallization expertise.
Engineered at the intersection of data science and structural biology, the Berkeley Screen captures the chemical conditions most strongly correlated with successful crystal formation across thousands of high-resolution Protein Data Bank structures. By identifying ions, buffers, precipitants, and small molecules frequently observed in electron density maps, the screen pinpoints the solution components that truly shape crystal packing.
Widely adopted by researchers at the Joint BioEnergy Institute and the Berkeley Center for Structural Biology, the Berkeley Screen has contributed to numerous PDB entries and publications—demonstrating real-world impact across diverse protein targets.
Why Researchers Choose the Berkeley Screen
Data-driven design: Built from statistical correlations between crystallization conditions and solved structures.
Scientifically validated: Components observed directly in electron density maps highlight their functional roles in crystal formation.
Proven performance: Successfully used in high-throughput crystallography pipelines, enabling rapid lead conditions for challenging targets.
Broad applicability: A versatile, general-purpose screen that complements and enhances existing commercial options.
Whether you're bootstrapping initial crystallization trials or expanding your toolbox for difficult targets, the Berkeley Screen offers a powerful, thoughtfully engineered starting point—bringing clarity and efficiency to one of structural biology’s most unpredictable steps.
In most cases, CrysAlisPro automatically determines the correct space group. However, challenging datasets may require the user’s crystallographic expertise. GRAL, the space-group determination module within CrysAlisPro, provides tools for this purpose. You can access GRAL by selecting manual space group determination during data reduction with options, or by enabling it before data refinalization (Figure 1).
Figure 1: Finalization window. Select “interactive” in the Space group and AutoChem tab to start GRAL after refinalization.
When GRAL launches after data finalization, it first displays the loaded .hkl file. In the Settings tab, you can adjust parameters such as the number of forbidden reflections allowed, the weighting scheme for space group preferences and the error for lattice selection (Figure 2).
Figure 2: GRAL Settings tab.
Next, select the centering based on the number of lattice exceptions for each option. GRAL will then transform the dataset to the Niggli cell. After this step, you can choose the crystal lattice from either the best matches or the full list of possible lattices (Figure 3). The centering can then be readjusted in the following tab, if needed.
Figure 3: GRAL Lattice tab. The lattice tolerance can be readjusted.
In the next tab, GRAL compares the experimental <E²-1> values with the expected acentric and centric distributions to determine whether the space group is likely centrosymmetric (Figure 4).
Figure 4: GRAL <E2-1> tab. The closest matches to the experimental values are indicated with <>.
The next tab is Space group selection. Here, systematic absence violations are listed according to both their number and whether their intensities fall below or above 3σ. GRAL suggests the most probable space groups based on the current settings. When the correct choice is not immediately clear, the Advanced space group selection tool can assist (Figure 5).
Figure 5: GRAL Space group tab with access to Advanced space group selection and the HKL viewer.
In the Advanced space group selection window, you can evaluate symmetry operations for each axis. GRAL displays all remaining compatible space groups, and the R(int) button calculates R(int) values for these candidates (Figure 6).
Figure 6: Advanced space group selection window.
For visual inspection of extinction conditions and their exceptions, use the HKL viewer. Selecting a space group overlays its expected systematic absences onto the diffraction data. This can be used to check if they agree with each other. If a space group is already chosen when opening the viewer, its absences automatically appear as red crossed, while violations are shown as yellow, orange or red squares depending on the intensity of the reflections. Different zones can be examined, color-coding thresholds adjusted, and symmetry elements manually toggled (Figure 7).
Figure 7: HKL viewer. Systematic absences from different space groups can be overlaid on the experimental diffraction data to assess consistency.
Once the space group selection is finalized and a chemical composition has been entered, the .ins file can be generated in the Ins-file tab.
Caroline Criado Perez’s Invisible Women: Exposing Data Bias in a World Designed for Men was first published in 2019, but it’s just as relevant today as it was six years ago. It might even be more relevant, given that many of the biases in Big Data that Perez outlines have impacted the development of omnipresent artificial intelligence technology trained by this inherently skewed data.
Perez breaks male-centric data biases into several categories: everyday life, work, product design, medicine, public life, and even natural disasters. Perez deftly weaves historical examples and statistics, digesting the data for the reader with clear and numerous examples of male-centric thinking resulting in less than positive outcomes for women. Perez’s prose is so energetic, reading Invisible Women feels like having an engaging discussion with a professor during office hours.
If you are a woman, many of the revelations in Invisible Women may seem like common sense. You might find yourself nodding along as you read, relating to the numerous examples of male-centric data bias in all aspects of your life. Why are iPhones too big for the average woman’s hand? They were designed for a man’s much larger average hand. Why is there always a massive queue for the ladies’ room and never a queue for the men’s room? Urinals take up less space than toilet stalls, so more men can relieve themselves at once in a men’s room with the same square footage as a ladies’ room. Why does the unisex one-size-fits-all sweatshirt I bought at a sporting event not fit me properly? Because unisex one-size-fits all usually means it was designed to fit male anatomy, not female anatomy.
If you are a man, take some notes and when you finish the book, encourage your male colleagues and friends to read it.
