IUCr journals

Coherent X-ray diffractive imaging of protein crystals

J. Synchrotron Rad. (2008). 15, 576-583 (doi.org/10.1107/S0909049508029439)

[X-ray diffractive imaging of proteins]
The new synchrotron radiation technique of coherent X-ray diffractive imaging using diffraction at a Bragg peak has been applied to the study of micrometer-sized protein crystals. Under coherent conditions, fringes appear on the Bragg peak, which are related to the crystal shape. In the highlighted work, the two-dimensional shape of the crystal was recovered from the diffracted intensity alone, using a real-space 'support' constraint. While radiation damage was a key limitation, this demonstration paves the way to the study of nanocrystals at free-electron laser sources, such as the Linac Coherent Light Source in 2009.

S. Boutet and I. K. Robinson