A Strong Link Between Organic Chemistry and Chemical Crystallography Started a Century Ago

The article sheds light on some historical crossings of organic chemistry and chemical crystallography. It connects past and present bringing into the focus Prof. Kata Mlinarić-Majerski’s research. An impact of structural chemistry on organic synthesis and reactivity is shown. X-ray structure analysis was established as a unique method to determine the composition and architecture of synthetic and natural organic molecules, already in the second decade of the last century; some of historical and scientific milestones are shown. Numerous controversies were solved, when intriguing molecular structures had been determined and the nature of chemical bond was clarified. An absolute structure (chirality) determination using an anomalous dispersion of X-rays was an important step forward, particularly in pharmaceutical industry. Structural data provided by X-ray crystallography, stored by Cambridge Structural Data Centre have been of great impact on many areas of science. They are closely related to intra- and intermolecular forces and structure/function correlations directing us to synthesis of compounds with designed properties. The developments of supramolecular chemistry, crystal engineering, materials science, and most of all of molecular machines have been assisted by chemical crystallography. The essay does not aim to review the complete scientific opus of Prof. K. Mlinarić-Majerski but it is focused on some of the highlights of her research. The interdisciplinary approach in her research is related to the use of X-ray structural analysis to define molecular architecture, conformational chirality, conformational isomerism, and get insight into reaction paths, interactions governing molecular assembling, and to recognise chemical properties of new compounds. In these researches the X-ray crystallographers were involved. This work is licensed under a Creative Commons Attribution 4.0 International License

Surveys: Crystallography, the Interdisciplinary Science of 21st Century: XX Congress of International Union of Crystallography, Florence 23-31. 08. 2005

Svjetski kongres kristalografa, koji se redovito održava svake treće godine od završetka Drugog svjetskog rata, jasno pokazuje aktualna usmjerenja i rezultate izrazito interdisciplinarne, tek nepuno stoljeće “stare” znanosti. To obiljeÞje došlo je do izražaja i na ovogodišnjem skupu u Firenci, koji je izborom programa i predavača privukao više od 2200 znanstvenika iz cijelog svijeta. Estetskom doživljaju tog skupa pridonijela je bogata renesansna baština toskanske prijestolnice. OdžÞano je 36 plenarnih (keynote) predavanja uključujuži kao predavače nobelovce R. Hoffmanna i H. Krotoa. Usporednih 98 mikrosimpozija pratila su predavanja i posteri. Bila su očita dva naglašena usmjerenja u istraživanju: proteinska struktura i funkcija i biološki aktivne male molekule (npr. nastajanje i struktura amiloidnih proteina, vezano uz Alzheimerovu bolest) te strukture i svojstva novih materijala (npr. dizajn Li-baterija, mikrostruktura materijala, nukleacija i rast zrna, ponašanje materijala pri visokim i niskim temperaturama i visokim tlakovima). Kongres je pokazao snažan razvoj novih eksperimentalnih tehnika i usavršavanje postojećih, što se ponajprije odnosi na primjenu sinkrotrona – izvora većeg intenziteta (8 GeV) u difrakcijskim mjerenjima imikroizvorima promjera 1mm – 1 µm (za rad s malim uzorcima) – kao i na renesansu neutronske difrakcije i primjenu krioelektronske mikroskopije u raspoznavanju slike makromolekula. Primjena difrakcijskih metoda u identifikaciji spojeva i razlièitih materijala nije novina, ali kolièine koje se mogu detektirati zapanjujuæe su male (nekoliko µg), što se veæ uvelike primjenjuje u forenzici, medicinskoj dijagnostici, znanosti o okolišu, arheologiji i nizu drugih podruèja. Uz moderne difrakcijske uređaje, opremljene podesnim kolimirajućim sustavima, osjetljivim detektorima te pratećim kriouređajima za hlađenje uzoraka i detektora, neprestance se pomiču granice mogućeg, pridonoseći točnosti, brzini i kvaliteti mjerenja. Razvoj pratećeg softvera i računala, uključujući diskusije o “grid computingu”, također su bili predmetom rada navedenog skupa

Jerome Karle, Nobel Laureate in Chemistry (1918–2013)

BiografijaBiograph

(Bio)Crystallography at the Turn of the Millennium

This review is focused on the present status of X-ray crystallography and its impact on Chemistry and the life Sciences. The discovery of the DNA double-helix structure from a fibre X-ray diagram in 1953 marked the last century, whereas the human genome project (to be completed in the year 2003, the 50-th anniversary of Crick\u27s and Watsons discovery) and the proteomics will open the new millennium. The crystal structure determinations of very complex biological assemblies such as viruses and ribosomes illustrate the power of contemporary X-ray structure analysis. The historical background is given, which touches on some of the important steps from the early days of the discovery of X-rays. The advanced and new methods and technologies of the modern era, such as third-generation synchrotrons, sensitive area detectors, up-to date Computer technologies with Computer graphics, cryotechniques, micro-crystallization methods, and genetic engineering, ali contributing to the development of X-ray crystallography, are evaluated in separate paragraphs. Some examples that illustrate the power of the methods are selected from the contemporary research in the field. Systematics of known crystal structures of small molecules and macromolecules and their assemblies collected over the years has developed our perception of the nature of the Chemical bond, and the interactions between atoms and molecules, which determine the Chemical, physical, and biological properties. This fundamental knowledge enables structure and property predictions, useful in many branches of Science and technology. A method, starting with the structure of table salt, has developed into a very fine tool for looking into complex living systems. Time-resolved crystallography and cryo-electron microscopy are capable of recording biological events and they inform us about the dynamics of enzymes and living cell activities. In combination with bioinformatics, very fast events, recorded experimentally or proposed theoretically, can be interpreted by the methods of molecular dynamics simulations. The vivid interplay of ideas coming from different Scientific fields and technologies has led to Capital discoveries, which have opened roads to new disciplines, such as molecular genetics and molecular medicine. These two branches, in particular, enriched by findings on DNA and protein structures, can provide efficient therapies for many diseases, health prevention, and reduce ageing problems. Our views on the nature of the Chemical bond have been revised and our horizons will be extended and clearer in the years to come. Applying an ethical approach in Science, humanity will learn how to improve the quality of life all over the world