BREAKING NEWS: Rigaku Corp. and Agilent Technologies Announce Rigaku to Acquire Agilent's X-Ray Diffraction Business

TOKYO and SANTA CLARA, Calif., March 30, 2015 – Rigaku Corp. and Agilent Technologies Inc. (NYSE: A) today announced an agreement for Rigaku, a privately held scientific instrumentation company headquartered in Tokyo, to acquire Agilent's X-ray diffraction (XRD) business.

Formerly known as Oxford Diffraction within Varian when that company was acquired by Agilent in 2010, the XRD group is a key manufacturer of single-crystal X-ray instruments for the global chemical crystallography market.

"The acquisition of Agilent's X-ray crystallography business represents a significant step in the expansion of our single-crystal X-ray business," said Hikaru Shimura, Rigaku President and CEO. "By combining Agilent's XRD business with Rigaku's expertise in protein crystallography, we will be able to leverage the best technologies from both groups to provide our current and future customers with world-class solutions for single-crystal analysis."

"This agreement is a positive development for the XRD business," said Patrick Kaltenbach, President, Agilent Life Sciences and Applied Markets Group. "I am confident that Rigaku will provide excellent support to grow the XRD business with complementary technology and the expertise of a highly talented team."

Rigaku plans to combine XRD with its existing crystallography business to form a new business unit. XRD products will continue to be developed and produced at existing factories in Poland and Japan.

The transaction is expected to be final May 1, 2015, subject to local laws and customary closing conditions. No financial terms were disclosed.

Crystallography in the news

March 2, 2015. A team lead by Janos Hajdu at Uppsala University, in Sweden, have demonstrated that it is possible to reconstruct the three-dimensional structure of a virus from a very large number of diffraction patterns collected from a sequence of randomly oriented single viruses.

March 2, 2015. A novel nucleating agent that builds on the concept of molecularly imprinted polymers (MIPs) could allow crystallographers access to proteins and other biological macromolecules that are usually reluctant to form crystals. The semi-liquid non-protein agent is reported by UK scientists.

March 4, 2015. Scientists at The Scripps Research Institute (TSRI) have published a pair of studies showing how the primary protein responsible for multidrug chemotherapy resistance changes shape and reacts to therapeutic drugs. The findings were published recently in two papers: a study in the journal Structure co-led by Bridget Carragher, a professor at TSRI with a joint appointment at the New York Structural Biology Center, and a paper in Acta Crystallographica Section D co-led by Geoffrey Chang, professor in the UC San Diego Skaggs School of Pharmacy and Pharmaceutical Sciences.

March 4, 2015. Big Pharma: Taking a Drug from Theory to Research and Development. Did you know that it can take up to 15 years to develop one new medicine? And out of the multiple new medicines being created only 10 percent reach the clinical trials phase, with only one of five ever being approved for human use?

March 8, 2015. The scientific literature has long been skewed by a preponderance of positive results, largely because journals are keen to nurture their reputations for publishing significant, exciting research ??? new discoveries that change the way we think about the world. They have tended to look askance at manuscripts reporting beautiful hypotheses undone by the ugly fact of experimental failure.

March 18, 2015. A clearer understanding of the origin recognition complex (ORC) ??? a protein complex that directs DNA replication ??? through its crystal structure offers new insight into fundamental mechanisms of DNA replication initiation. This will also provide insight into how ORC may be compromised in a subset of patients with Meier-Gorlin syndrome, a form of dwarfism in humans.

March 19, 2015. Unique X-ray laser innovation developed at the Department of Energy's SLAC National Accelerator Laboratory may make it easier and faster for scientists to fully map medically important proteins whose structures have remained stubbornly out of reach. It involves hitting samples with pairs of precisely tuned X-ray laser pulses of different colours, or wavelengths. When the pulses hit at the same time, they can give scientists a more detailed 3-D view of the sample???s structure.

March 23, 2015. Saccharin, the artificial sweetener that is the main ingredient in Sweet 'N Low??, Sweet Twin?? and Necta??, could do far more than just keep our waistlines trim. According to new research, this popular sugar substitute could potentially lead to the development of drugs capable of combating aggressive, difficult-to-treat cancers with fewer side effects.

March 26, 2015. Intrinsically disordered proteins are associated with neurodegenerative changes, cardiovascular disorders and diseases such as diabetes and cancer. One intrinsically disordered protein, beta-catenin, is of particular interest to researchers at the U.S. Dept. of Energy (DOE)???s Oak Ridge National Laboratory (ORNL), where they will be conducting neutron scattering and supercomputing studies to further uncover its role in cancer.

March 26, 2015. Ada E. Yonath: A woman???s journey in science. When she won the Nobel Prize in Chemistry in 2009, Ada E. Yonath was hailed around the world as the first Middle Eastern woman, the first Israeli woman, and the fourth woman in history to be granted the award. But for Professor Yonath herself, there was nothing special about a woman winning a Nobel.

Product spotlight: BioSAXS-2000

Rigaku's BioSAXS-2000 SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-2000 takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-2000 can be mounted on the open port of a Rigaku rotating anode X-ray generator, taking full advantage of existing infrastructure, or it can be mated to a Rigaku microfocus sealed tube X-ray source. The BioSAXS AUTO configuration incorporates two time-saving features: an Automatic Sample Changer for unattended overnight operation and an Automatic Analysis Pipeline based on the world standard ATSAS package from EMBL Hamburg. Visit Rigaku.com for more information on the BioSAXS-2000.

Lab spotlight: Structural Studies Division at MRC Laboratory of Molecular Biology

Prof. Venki Ramakrishnan,
Structural Studies Division,
MRC Laboratory of Molecular Biology,
Hills Road, Cambridge,
CB2 0QH, England

As part of the Centre for Structural Biology, the X-ray Crystallography Facility serves the macromolecular crystallography community at Imperial College London. About 75 users from twenty-five research groups come to the facility on a regular basis to crystallize the proteins they study, optimize obtained hits, test diffraction and cryo-conditions, and collect diffraction data. The projects cover bacterial pathogenesis, molecular plant biology, membrane biology, molecular mechanisms of disease, and the understanding of protein crystallization.

Venki???s research group is interested in the structure and function of the ribosome, the large protein-RNA complex that synthesizes proteins using genetic instructions encoded in the mRNA template. Following the determination of the 30S subunit and its complexes with antibiotics and ligands in 2000, and the entire 70S ribosome with mRNA and tRNA ligands in 2006, they have determined high-resolution structures of many functional states of the ribosome. These structures have shed light on the role of the ribosome in decoding of mRNA, peptidyl transfer, translocation and termination. They have also elucidated complexes of the ribosome involved in stress response and quality control. Finally, they are beginning work on trying to understand translational initiation and termination in eukaryotes.

Useful link: Crystallography at 100

Science's Special Issue on Crystallography at 100, published in 2014, celebrates the insights gained from structural studies that have revolutionized our understanding of chemical and biological systems, leading to the award of 29 Nobel Prizes for scientific achievements related to, or involving the use of, crystallography.

At least 10% shorter C???H bonds in cryogenic protein crystal structures than in current AMBER forcefields. Pang, Yuan-Ping. Biochemical & Biophysical Research Communications. Mar2015, Vol. 458 Issue 2, p352-355. 4p. DOI: 10.1016/j.bbrc.2015.01.115.

New insights into the meaning and usefulness of principal component analysis of concatenated trajectories. Pierdominici-Sottile, Gustavo; Palma, Juliana. Journal of Computational Chemistry. Mar2015, Vol. 36 Issue 7, p424-432. 10p. DOI: 10.1002/jcc.23811.

Proteogenomics: emergence and promise. Faulkner, Sam; Dun, Matthew; Hondermarck, Hubert. Cellular & Molecular Life Sciences. Mar2015, Vol. 72 Issue 5, p953-957. 5p. DOI: 10.1007/s00018-015-1837-y.

Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine. Ling Qin; Kufareva, Irina; Holden, Lauren G.; Chong Wang; Yi Zheng; Chunxia Zhao; Fenalti, Gustavo; Huixian Wu; Gye Won Han; Cherezov, Vadim; Abagyan, Ruben; Stevens, Raymond C.; Handel, Tracy M. Science. 3/6/2015, Vol. 347 Issue 6226, p1117-1122. 6p. DOI: 10.1126/science.1261064.

Bacteriorhodopsin: Would the real structural intermediates please stand up? Wickstrand, Cecilia; Dods, Robert; Royant, Antoine; Neutze, Richard. BBA - General Subjects. Mar2015, Vol. 1850 Issue 3, p536-553. 18p. DOI: 10.1016/j.bbagen.2014.05.021.

The rate of cis-trans conformation errors is increasing in low-resolution crystal structures. Croll, Tristan Ian. Acta Crystallographica: Section D. Mar2015, Vol. 71 Issue 3, p706-709. 4p. DOI: 10.1107/S1399004715000826.

Xlink Analyzer: Software for analysis and visualization of cross-linking data in the context of three-dimensional structures. Kosinski, Jan; von Appen, Alexander; Ori, Alessandro; Karius, Kai; M??ller, Christoph W.; Beck, Martin. Journal of Structural Biology. Mar2015, Vol. 189 Issue 3, p177-183. 7p. DOI: 10.1016/j.jsb.2015.01.014.

Radiation damage to nucleoprotein complexes in macromolecular crystallography. Bury, Charles; Garman, Elspeth F.; Ginn, Helen Mary; Ravelli, Raimond B. G.; Carmichael, Ian; Kneale, Geoff; McGeehan, John E. Journal of Synchrotron Radiation. Mar2015, Vol. 22 Issue 2, p213-224. 12p. DOI: 10.1107/S1600577514026289.

Analysis of the Radiation-Damage-Free X-ray Structure of Photosystem II in Light of EXAFS and QM/MM Data. Askerka, Mikhail; Vinyard, David J.; Jimin Wang; Brudvig, Gary W.; Batista, Victor S. Biochemistry. 3/10/2015, Vol. 54 Issue 9, p1713-1716. 4p. DOI: 10.1021/acs.biochem.5b00089.

Automated de novo phasing and model building of coiled-coil proteins. R??misch, Sebastian; Lizatovic, Robert; Andr??, Ingemar. Acta Crystallographica: Section D. Mar2015, Vol. 71 Issue 3, p606-614. 9p. DOI: 10.1107/S1399004714028247.

The fickle P value generates irreproducible results. LG Halsey, D Curran-Everett, SL Vowler and GB Drummand. Nature Methods. Vol 12, 2015, pp 179-185. DOI: 10.1038/nmeth.3288.

Local and macroscopic electrostatic interactions in single α-helices. Baker, Emily G; Bartlett, Gail J; Crump, Matthew P; Sessions, Richard B; Linden, Noah; Faul, Charl F J; Woolfson, Derek N. Nature Chemical Biology. Mar2015, Vol. 11 Issue 3, p221-228. 8p. DOI: 10.1038/nchembio.1739.

Conformational Change from Rigid Rod to Star: A Triple-Helical Peptide with a Linker Domain at the C-Terminal End. Ken Terao; Kazunori Mizuno; B??chinger, Hans Peter. Journal of Physical Chemistry B. Mar2015, Vol. 119 Issue 9, p3714-3719. 6p. DOI: 10.1021/jp5129172.

Comparative structural analysis of the caspase family with other clan CD cysteine peptidases. McLuskey, Karen; Mottram, Jeremy C. Biochemical Journal. 3/1/2015, Vol. 466 Issue 2, p219-232. 14p. DOI: 10.1042/BJ20141324.

Repeat-Proteins Films Exhibit Hierarchical Anisotropic Mechanical Properties. Carter, Nathan A.; Grove, Tijana Zarkovic. Biomacromolecules. Mar2015, Vol. 16 Issue 3, p706-714. 9p. DOI: 10.1021/bm501578j.

Radiation damage to macromolecules: kill or cure? Garman, Elspeth F.; Weik, Martin. Journal of Synchrotron Radiation. Mar2015, Vol. 22 Issue 2, p195-200. 6p. DOI: 10.1107/S160057751500380X.

Structure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modification. Kolaj-Robin, Olga; McEwen, Alastair G.; Cavarelli, Jean; S??raphin, Bertrand. FEBS Journal. Mar2015, Vol. 282 Issue 5, p819-833. 15p. DOI: 10.1111/febs.13199.

Structure of a complex of uridine phosphorylase from Yersinia pseudotuberculosis with the modified bacteriostatic antibacterial drug determined by X-ray crystallography and computer analysis. Balaev, V.; Lashkov, A.; Gabdoulkhakov, A.; Seregina, T.; Dontsova, M.; Mikhailov, A. Crystallography Reports. Mar2015, Vol. 60 Issue 2, p217-226. 10p. DOI: 10.1134/S1063774515020030.

Structures of Eukaryotic Ribosomal Stalk Proteins and Its Complex with Trichosanthin, and Their Implications in Recruiting Ribosome-Inactivating Proteins to the Ribosomes. Choi, Andrew K. H.; Wong, Eddie C. K.; Ka-Ming Lee; Kam-Bo Wong. Toxins. 2015, Vol. 7 Issue 3, p638-647. 10p. DOI: 10.3390/toxins7030638.

Crystal structure of a periplasmic solute binding protein in metal-free, intermediate and metal-bound states from Candidatus Liberibacter asiaticus. Sharma, Nidhi; Selvakumar, Purushotham; Bhose, Sumit; Ghosh, Dilip Kumar; Kumar, Pravindra; Sharma, Ashwani Kumar. Journal of Structural Biology. Mar2015, Vol. 189 Issue 3, p184-194. 11p. DOI: 10.1016/j.jsb.2015.01.012.

Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins. Liu, Liang; Chen, Jiyun; Yang, Bo; Wang, Yonghua. Biochemical & Biophysical Research Communications. Mar2015, Vol. 458 Issue 2, p429-434. 6p. DOI: 10.1016/j.bbrc.2015.01.134.

Crystal structure of the effector protein HopA1 from Pseudomonas syringae. Park, Yangshin; Shin, Inchul; Rhee, Sangkee. Journal of Structural Biology. Mar2015, Vol. 189 Issue 3, p276-280. 5p. DOI: 10.1016/j.jsb.2015.02.002.

Helical assemblies: Structure determinants. Kurochkina, Natalya A.; Iadarola, Michael J. Journal of Theoretical Biology. Mar2015, Vol. 369, p80-84. 5p. DOI: 10.1016/j.jtbi.2015.01.012.

Structural and functional analysis of two universal stress proteins YdaA and YnaF from Salmonella typhimurium: possible roles in microbial stress tolerance. Bangera, M.; Panigrahi, R.; Sagurthi, S.R.; Savithri, H.S.; Murthy, M.R.N. Journal of Structural Biology. Mar2015, Vol. 189 Issue 3, p238-250. 13p. DOI: 10.1016/j.jsb.2015.01.003.

Prediction of protein structural class using tri-gram probabilities of position-specific scoring matrix and recursive feature elimination. Tao, Peiying; Liu, Taigang; Li, Xiaowei; Chen, Lanming. Amino Acids. Mar2015, Vol. 47 Issue 3, p461-468. 8p. DOI: 10.1007/s00726-014-1878-9.

Identifying and quantifying radiation damage at the atomic level. Gerstel, Markus; Deane, Charlotte M.; Garman, Elspeth F. Journal of Synchrotron Radiation. Mar2015, Vol. 22 Issue 2, p201-212. 12p. DOI: 10.1107/S1600577515002131.

NuProPlot: nucleic acid and protein interaction analysis and plotting program. Pradhan, Lagnajeet; Nam, Hyun-Joo. Acta Crystallographica: Section D. Mar2015, Vol. 71 Issue 3, p667-674. 8p. DOI: 10.1107/S1399004715000139.

Book review: Most Wanted Particle: The Inside Story of the Hunt for the Higgs, the Heart of the Future of Physics

     by Jon Butterworth
     The Experiment, LLC, New York, 2014. ISBN 978-1-61519-246

Jon Butterworth???s Most Wanted Particle is an often very funny first-person account of his involvement in the experimental confirmation of the Higgs boson at the Large Hadron Collider (LHC) near Geneva, Switzerland in 2012. Dr. Butterworth was involved in developing algorithms to analyze the ???jets??? of particles that are produced in the proton-proton (or other) collisions and how their properties can provide indirect evidence for short-lived and massive bosons.

The tale is interwoven with many personal opinions and anecdotes that illustrate the ???two steps forward, one step back??? nature of the endeavor. These include the heartbreaking accidental explosion of superconducting magnets in the LHC due to a welding error just after the initial startup that led to a yearlong delay. The author shows his painful empathy for excited young physics students who had to deal with not taking data for a year.

Separate scientific sections explain both the Standard Model of particle physics and the gaping hole that could be filled by proving the existence of the boson predicted by Peter Higgs and his colleagues that imparts mass on all fundamental particles. Butterworth explains the statistical criteria that had to be painstakingly agreed upon to actually call the data evidence for a ???Higgs boson???.

The reader will come to appreciate the incredible long-range planning, engineering, computing, and infrastructure (just thinking of the plumbing, safety and administrative aspects makes one???s head hurt) required to build and maintain a giant instrument to examine matter at its tiniest and most powerful scale.

An excellent aspect of the book is how, as a leader and representative for the ATLAS detector at LHC, Butterworth had to confront via social and other communication media the constant tension in our culture between funding hugely expensive efforts like the LHC and the inability to say exactly when and how discoveries made there will benefit humanity directly. On that note, Butterworth reminds us that the world-wide-web is a direct result of Tim Berners-Lee figuring out how to immediately share data from large particle accelerator experiments with collaborators across the globe.

As an occasional user of synchrotron light sources, this reviewer is always in awe of what biologists, chemists, and materials scientists have been able to accomplish due to these large physics-based particle accelerators and their spin-off applications. A nice teaching aspect of the book is how Butterworth explains the requirements of wavelength and resolution for probing matter at the level of quarks, gluons, and Higgs bosons in a way that I could relate to as an X-ray crystallographer.

Butterworth???s account shows that the Higgs experiment was the result of brilliant theory that makes testable hypotheses (once the energy to test them is accessible), enormous technical and logistical mastery, massive public support (hence funding), teamwork that keeps the ???eyes on the prize???, and dogged persistence. His enthusiasm and emotional highs and lows are infectious, including funny anecdotes about scientific meetings, chance encounters, and dealing with the public. Sometimes I found the writing to be a bit rambling due to many digressions, and it was not hard to become lost in the nomenclature. I would recommend the book to scientists or nerdy types interested in fundamental discoveries, but I am not sure that a non-scientist would enjoy it as much.

Joseph D. Ferrara, Ph.D.
Chief Science Officer