Kate Stafford’s favorite structure is:

Ribonuclease H1 (2QK9)

Ribonuclease H1 (2QK9)

Source: Kate Stafford

Why?

It’s my PhD protein! RNase H is an enzyme that cleaves DNA-RNA hybrids that is found in all domains of life. RNases H from mesophilic and thermophilic bacteria were among the first homologous structures solved from organisms adapted to different temperatures and are structurally very similar despite large differences in enzymatic activity. My work used molecular dynamics simulations to interpret NMR measurements of these proteins’ internal dynamics to better understand the relationship between motion, function, and thermal adaptation.

The PDB code cited above (2QK9) is that of the human RNase H homolog, which was solved in the presence of a hybrid substrate.

RNase H is essential in higher eukaryotes, so everyone reading this has a functional one. It is also essential for the proliferation of retroviruses, making selective inhibitors of the retroviral RNase H domain a potential drug target for novel HIV treatments.

The attached photo is the human RNase H 3D printed with Shapeways. —Kate Stafford


Ashutosh Jogalekar’s favorite structure is:

Alpha hemolysin

Alpha hemolysin

Source: Wikipedia (PDB code 7ahl)

Why?

Alpha hemolysin is one of the very few protein structures that’s not only breathtakingly pretty and intricate but which is also the epicenter of a true technological breakthrough.

The entire structure resembles a flower and traverses a membrane. Beta sheets run along each other to form a 14-strand beta barrel ‘stem’ while other beta sheets line up next to each other at the rim to form the ‘petals’. Both these substructures enclose a remarkable, 100 A long solvent-filled channel. And most impressively, all these subunits self-assemble.

The practical reason why alpha hemolysin is so fascinating is because it is the linchpin of next generation DNA sequencing technology. By utilizing the solvent-filled channel as a nanopore, researchers are threading DNA strands through it and sequencing individual nucleotide bases by looking at minute changes in electrical current across the pore. The technology has already been commercialized and promises to reduce both the cost and time of sequencing.

Alpha hemolysin is thus one of the most perfect examples of combining elegant form with breakthrough technological function. It’s as good an example as I know of nature’s unsurpassed ability to create both beauty and utility in one fell swoop. —Ashutosh Jogalekar


Pennarun’s favorite structure is:

Snowflakes hexagonal struture

Snowflakes hexagonal struture

Source: http://en.wikipedia.org/wiki/X-ray_crystallography#mediaviewer/File:Snowflake8.png

Why?

Water is one of the simplest molecule on earth and essential to life. Well known molecule, it is in the same time a molecule that still not completely known when grouped with other water molecule. Snowflakes show broad number of structures, from which mechanical behavior will depend. Macroscopic mechanical behavior of snow, especially in montains, depends then only of the weak very small hydrogen bonds. In the same time not so weak as USA think to use it with wood fibers to build armor for warships as strong as metallic ones during the WWII. —Pennarun


Marc Armbrster’s favorite structure is:

CuAl2

CuAl2

Source: My PhD thesis :-)

Why?

The intermetallic compound CuAl2 helped to reveal that the chemical bonding depends on the elements in a series of isostructural compounds and not on the crystal struture. Besides, it is one of the best examples that simple metals like copper and aluminum can form beautiful crystal structures upon compound formation! —Marc Armbrster


Xin Su’s favorite structure is:

Insulin/4-hydroxybenzamide on space mission STS-60

Insulin/4-hydroxybenzamide on space mission STS-60

Source: PDB

Why?

Despite many insulin crystal structures you may find in the Protein Data Bank, this one is extraterrestrially exotic. In addition to its exquisite beauty, grown under microgravity aboard the Space Shuttle Discovery, the high-quality crystal enabled scientists to reveal the fine details about drug-insulin interactions, which would have been impossible with earth-grown ones. —Xin Su


Kelly Tyrrell’s favorite structure is:

MreB

Evolution of the cytoskeleton JCB

Source: The Journal of Cell Biology

Why?

Prior to the advent of x-ray crystallography, one of the defining characteristics of prokaryotes was “lacks a cytoskeleton.” However, when the crystal structure of bacterial MreB was found, scientists discovered that MreB and eukaryotic actin “look” nearly identical. It turned that notion completely upside down, rewriting textbooks, and scientists have been studying these homologs – and the evolutionary origins of these proteins – ever since. —Kelly Tyrrell


Miranda Paley’s favorite structure is:

1FKA

1fka_asr_r_250

Source: PDB

Why?

Because: it’s the freaking ribosome! While later structures provided better resolution, this structure is the hallmark of visionary Ada Yonath’s career. She was ridiculed for so many years about trying to crystallize the ribosome, and she finally got it! The additional work on the paper modeling in tetracycline to show its mode of action and to further validate the solution to the structure is also well done. —Miranda Paley


George Oh’s favorite structure is:

i-YbCd5.7

Why?

There is such high symmetry – concentric shapes within shapes, starting with platonic solids and going into bigger polyhedra to fit the number of atoms. The shapes are also interwoven with each other, and the viewer can find a multitude of shapes of all sorts of symmetry. It’s like playing with shape tiles in elementary school, but in 3d! —George Oh


Stephanie Taylor’s favorite structure is:

DNA

Stephanie Taylor

Source: Stephanie Taylor

Why

DNA says so much in a single picture. First, getting students to have an idea of what x-ray crystallography IS can be difficult. They have been seeing this odd black and white picture in chapters on DNA in their textbooks since high school, so it obviously has a biology connection.

Second, it connects the importance of the contribution of women in science. Rosalind Franklin not only discerned that the phosphate backbone was on the OUTSIDE of the structure, she also was among the first to crystallize the B form of DNA, which created clearer x-ray diffraction patterns and is more biologically relevant.

Finally, though it is well known, DNA is far from a cliche molecule. Its versatility and stability fascinate biologists, chemists, engineers, and physicists. Every field has a niche for it.

I am certain you will get this answer often, and for the best of reasons — while we have beautiful structures of many things of importance, you will find it difficult to find a scientist (amateur to professional) who is unfamiliar with the beauty of their own legacy and lineage: DNA. —Stephanie Taylor


Vito Capriati’s favorite structure is:

α-Lithiated oxirane

Lithiated_epoxide

Source: Chemical Science 2014, 5, 528-538

Why

This is the first crystallographic evidence for the structure of a highly reactive lithiated aryloxirane (t½ = 1.6 s at 157 K in THF). All operations were carried out under a nitrogen atmosphere at the temperature of 100 K. α-Lithiated oxiranes have long considered “fleeting” intermediates in the reaction of epoxides with strong bases, but have nowadays proven to be key synthons for asymmetric synthesis. They are small-ring heterocycles carrying a peculiar polarized Li-C bond which gives them the character of “carbenoids”, thereby exhibiting an amphiphilic behaviour, that is a nucleophilic as well as an electrophilic reactivity. In spite of their widespread use in synthetic strategies, however, information about the reactivity and structural features of these species were lacking before publishing these data. Indeed, It was as well long postulated that was an alkoxy carbene, in equilibrium with the lithiated epoxide, responsible of the carbene-like reactivity observed under certain experimental conditions. The knowledge of the solution and the solid structure of these intermediates may set the scene for future development in the field of α-lithiated epoxides and for controlling stereochemistry in C–C bond forming reactions onto an oxirane moiety. —Vito Capriati


Ombretta Masala’s favorite structure is:

Franklin’s famous “photograph 51” that finally revealed the helical structure of DNA

x-ray

Source: www.nobelprize.org

Why?

It was Franklin’s famous X-ray diffraction photo that finally revealed the helical structure of DNA to Watson and Crick in 1953.

It is my favourite because it solved the puzzle of the elusive structure of the DNA and I like the story behind. Franklin was robbed of recognition because Photo 51 enabled Watson, Crick, and Wilkins to deduce the correct structure for DNA, which they published in a series of articles in the journal Nature in April 1953 without Franklin. Franklin’s image of the DNA molecule was key to deciphering its structure, but only Watson, Crick, and Wilkins received the 1962 Nobel Prize in physiology or medicine for their work (Franklin died four years earlier and Nobel prizes aren’t awarded posthumously).

It is thought as one of the most well-known—and shameful—instances of a researcher being robbed of credit and in particular of a woman scientist who was snubbed due to sexism. —Ombretta Masala