While many celebrate the coming of a new year, with resolutions of fitness and growth, the United Nations Educational, Scientific, and Cultural Organization (UNESCO) strives towards a different goal: promoting science to the general public world-wide. 2014 has been marked as the International Year of Crystallography (ICYr). This project is a joint effort by the International Union of Crystallography and UNESCO, with the goal of promoting education on the importance of crystallography in science and in society.
X-ray crystallography is the examination of patterns in diffracted X-rays to determine the crystalline atomic structure of solids. Despite the small number of people who have heard of X-ray crystallography, its role in science and society as a whole is virtually unparalleled. Since the preliminary work of Johannes Kepler in ice crystal symmetry in 1611, the role of symmetry in nature has enthralled scientists. X-ray crystallography has led to the discovery of many properties of crystals.
Max von Laue was awarded the Nobel Prize in Physics in 1914 for the discovery that X-rays travelling through a crystal were diffracted in specific directions, and hence their behaviour depended on the nature of the crystal. These are the foundational experiments upon which the field of X-ray crystallography is built, and since von Laue’s discovery, over 45 scientists have received Nobel Prizes for work either directly or indirectly related to crystallography.
Among these accomplishments are many important discoveries: the discovery of the structure of penicillin, leading to the betterment of millions of lives; the control and processing of anti-viral drugs, since crystallography helps researchers study the effectiveness in binding to viruses; and perhaps most importantly, the crystallization process that makes that perfect piece of chocolate melt in your mouth, as naturally occurring forms are inedible.
At U of T, crystallographic research has led to the discovery of a molecule labelled penicillopepsin, which has been critical in improving the lives of those who suffer with AIDS. From medicine to confections, X-ray crystallography is the foundation of many life-saving and important medical and industrial applications.
The future of the field is very promising, with advancements predicted in efficient eco-friendly materials, and a possible solution to antibiotic resistant bacteria.
Current studies in crystallography seek to win the war against drug-resistant bacteria, also known as “superbugs.” Ada Yonath and colleagues are close to creating antibiotics to eliminate bacterial ribosomes while leaving those of humans unharmed. She won the Nobel Prize in 2009 for determining the structure of ribosomes in bacteria, without which bacteria could not survive.
The field of X-ray crystallography continues to contribute to advances in various disciplines, as the community of crystallography labs around the world expands. With the start of the IYCr, UNESCO hopes to achieve more global awareness of this crucial field, and hopes that in this new year, science will play a larger part in our lives than ever before.
Women in crystallography
As the International Year of Crystallography begins, The Varsity celebrates female crystallographers who have risen to prominence within the field, despite facing challenges to fit into the matrix of the scientific community — Emma Hansen
Dame Kathleen Lonsdale was a British scientist who made significant contributions to X-ray crystallography. Using X-ray diffraction methods, she discovered the structure of the benzene ring, settling a decades-long dispute.
Lonsdale attended a high school for boys in order to take courses in mathematics and science that were not offered at the girls’ high school. In 1927, Kathleen married Thomas Jackson Lonsdale. They were both scientists, Quakers, and pacifists. Evenings were spent doing science: Kathleen did her work on paper, and Thomas, working towards his doctorate, did experimental work in the kitchen.
Kathleen’s habit of working in the evenings continued even when she was jailed for a month for refusing to take part in civil defense activities, which would have been in conflict with her pacifist convictions.
She turned her cell into a laboratory with papers and instruments sent from colleagues. She was one of the first two female Fellows of the Royal Society, and she was the first woman to receive tenure at University College, London, where she was head of the Department of Crystallography. She was also the first female president of the International Union of Crystallography. Lonsdaleite, a form of carbon present in meteorites, bears her name.
Dorothy Hodgkin, a pioneer of protein crystallography, was described by her biographer as a brilliant scientist “whose humanity recognized no national boundaries.” Hodgkin was the first scientist to successfully use X-ray crystallography to study complex biomolecules. She confirmed the structure of penicillin, and later discovered the structure of vitamin B12 and insulin.
Hodgkin was the first female recipient of the Copley Medal, and the third female Nobel Laureate in Chemistry after Marie Curie and her daughter. Hodgkin also tutored Margaret Thatcher in chemistry and established a laboratory at Oxford. Throughout her constant struggle with rheumatoid arthritis, Hodgkin continued to excel at crystallographic research despite its delicate and precise nature. Hodgkin campaigned against nuclear weapons and supported scientists in developing countries in the later part of her career.
Franklin is best known for her X-ray diffraction work that led to the discovery of the structure of DNA. In the late 1940’s and early 1950’s, the race to discover the structure of DNA was on. Franklin, a physical chemist by training, worked with Maurice Wilkins in X-ray crystallography at King’s College. Meanwhile, Francis Crick and James D. Watson were working at Cavendish Laboratory at Cambridge.
The crystallographic images that Franklin produced were crucial to Crick and Watson’s discovery of the structure of DNA, although the Cambridge team did not have her permission to use the images, and she was not credited in their paper. Nonetheless, Franklin and Wilkin’s experimental work complemented Watson and Crick’s theoretical approach, and Crick, Watson, and Wilkins shared the 1962 Nobel Prize in Physiology or Medicine. Franklin had lost her life to cancer four years prior, but Wilkins recognized her “great ability and experience of X-ray diffraction” in his Nobel Lecture.
The academic environment during Franklin’s career was intensely hostile towards female scientists. Despite her significant contributions and her considerable skill, she did not receive fair recognition for her work at the time, and she was represented as incompetent and disagreeable in Watson’s memoir, The Double Helix. A biography of Franklin, as well as numerous protests against Watson’s portrait of Franklin by her colleagues and reviewers, helped to set her public image straight. Her tragically short life is now recognized as one of brilliant scientific achievement.
In her early career, Ada Yonath was labelled “the village idiot” for her unpopular ideas in biochemistry and structural chemistry. In 2009, she won a Nobel Prize for those same ideas, becoming the first Israeli woman to do so.
Yonath created Israel’s first biological crystallography laboratory at the Weizmann Institute, her alma mater. She sought to understand the structure of ribosomes, and was harshly criticized for pursuing her pioneering line of work. Yet she found success: she worked out the structure of the small ribosomal subunit using X-ray crystallography.
This work would prove to be essential to the study of antibiotic resistance. She shared the 2009 Chemistry prize with Venkatraman Ramakrishnan and Thomas A. Steitz, whose research had also led them to structural models of ribosomal subunits. Yonath was also the first female recipient of the Nobel Prize in Chemistry since Dorothy Hodgkin received the Prize in 1964.