With instruments like this, it will make the task of X-ray crystallography determination of protein structures much easier.
No, it won't. Two reasons:
1) You need "hard" X-rays for crystallography - with a wavelength similar to the chemical bond length. The maximum resolution you can achieve is equivalent to half the wavelength, and even that requires a complicated detector setup, so in practice you want a wavelength around 1 ? for crystallography. The wavelength of this device is 8?, which is fine for spectroscopy and small-angle scattering studies, but useless for crystallography. While I suspect the technology could be made to work at shorter wavelengths, this usually involves tradeoffs such as higher cost, higher energy consumption, etc.
2) The intensity of the source is far less than a synchrotron (let alone a free-electron laser). This means that data collection times will take far longer. At a synchrotron beamline, in favorable conditions, you can collect an entire data set in seconds (of course, the detector alone costs more than $1 million). Usually it's not quite that fast, but you don't need to wait days for your data - and you can hedge your bets by collecting data on as many crystals as possible.
A secondary reason is that the improvement in synchrotron beamline technology has also made them more accessible - much of the work is now done remotely using robotic sample changers. Being able to grow decent crystals in the first place is a far more limiting factor. And my impression is that beamtime isn't terribly difficult to get; people do still use home X-ray sources while they're waiting for beamtime, but most people are content to wait for the synchrotron to get the truly publishable data.
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