New setup enables EPR studies on tiny protein crystals
![An image showing the molecular structure of the [FeFe]-hydrogenase active site, the H-cluster](https://d2cbg94ubxgsnp.cloudfront.net/Pictures/100x67/1/9/3/501193_index_834443.jpg)
Experiments that normally takes five hours can now be done in just eight minutes
An electron paramagnetic resonance (EPR) method that works with nanolitre volume crystals could tease out new information about enzymes without the need for large and difficult to grow crystals.1 The technique, which is based on a special resonator geometry, can be used to perform EPR experiments on very small protein crystals such as those commonly used for x-ray crystallography. The new setup enables detailed studies on far more proteins than previously possible.