Chances are better than slim that this picture has popped up on your Tumblr dashboard (or elsewhere) during your recent internet wanderings. All that strange and beautiful life, present in just a single drop of seawater! A microscopic bestiary overflowing with life’s smallest oddities! Isn’t it amazing?
Just one problem: It’s not true.
This is certainly a collection of zooplankton (what we call non-photosynthetic plankton species), but it’s absolutely not from a single drop of ocean. As Miriam Goldstein explains at Deep Sea News, it’s from a volume more like that of a swimming pool, captured and concentrated in a special net that scientists use to survey these microscopic species. Check the link to find out more about why and how scientists collect these beautiful samples!
So who cares? What’s the difference if it’s a drop or if it’s a swimming pool? The problem is that we’re missing out on some very cool truth by lazily inserting some very cool lies. We don’t need to lie about how amazing nature is. The ocean is (quite literally) full of amazing life. We can celebrate that without inventing a story, right? Because the real story, the one that uses a beautiful image to connect us to actual scientific research, is awesome in its own right.
Although this image has gone viral recently, I posted it five months ago, wrong information and all. I didn’t check to make sure that what I posted was true, and that was my bad. I should do better. We all should.
Scientists have odious manners, except when you prop up their theory; then you can borrow money of them.
—Mark Twain, “As Concerns Interpreting the Deity”
"Anything becomes interesting if you look at it long enough.” - Gustavo Flaubert
"If one wanted to crush and destroy a man entirely, to mete out to him the most terrible punishment, all one would have to do would be to make him do work that was completely and utterly devoid of usefulness and meaning.” -Dostoevsky
"Where the needs of the world and your talents cross, there lies your vocation." -Aristotle
One U.S. Supreme Court justice referred to Netflix as “Netflick.” Another seemed not to know that HBO is a cable channel. A third appeared to think most software coding could be tossed off in a mere weekend.
Cross section of superconducting magnet wire etched with nitric acid (150x) (via Cross section of superconducting magnet wire etched with nitric acid | Brightfield | Nikon Small World)
s-c-i-guy asked: In Rosalind Franklin's crystallography experiment, how did the DNA strand not get destroyed by the high energy X-rays used?
I worked with crystallographers for like seven years, and I’m still convinced it’s 95% magic.
In x-ray crystallography experiments, you don’t shine the x-ray beam on one single DNA strand, or protein, or whatever it is you’re looking at. One DNA strand would certainly be obliterated by the beam, but not necessarily the crystal (although, often, the x-ray does annihilate your sample. That’s why you need more than one, which makes it even harder).
Instead of a single molecule, it’s a solid crystal, precipitated out of a complex solution of sometimes more than a dozen chemicals, with each crystal made of bajillions and bajillions of individual molecules arranged in an organized lattice. Different crystal structures, whether they are cubes, or tetrahedrons, or hexagonal pyramidal pentaglobs, will act differently in the beam. You don’t know in advance what you’re gonna get.
The protein crystals we used to look at back in my Ph.D. lab looked a lot like this:
Actually, if we’re being honest, they usually didn’t look like that. This is the sort of crystal you dream of. Most things aren’t quite this tidy when they crystallize.
When the x-ray beam is directed at the crystal, it diffracts (bounces off of) any atoms in its way. But x-rays have super-short wavelengths, and molecules are mostly empty space, so only a small fraction of the x-ray waves encounter an atom to bounce off of.
It’s the sum of ALL the rare bouncing events, in the entire crystal, organized into its repeating, ordered structure, that creates the x-ray dot pattern. Then the real fun begins, which as any x-ray crystallographer (and I am not one) will tell you, involves lots of math, and a fair bit of magic.
Oh, man. I spent some time as an undergrad trying to crystallize rhodopsin (before I discovered that people had been trying unsuccessfully for decades) and doing SEM measurements. What a nightmarish slog. I would have dreamed of a crystal like that.