TY  - JOUR
AU  - Ayyer, Kartik
AU  - Yefanov, Oleksandr
AU  - Oberthür, Dominik
AU  - Roy-Chowdhury, Shatabdi
AU  - Galli, Lorenzo
AU  - Mariani, Valerio
AU  - Basu, Shibom
AU  - Coe, Jesse
AU  - Conrad, Chelsie E.
AU  - Fromme, Raimund
AU  - Schaffer, Alexander
AU  - Dörner, Katerina
AU  - James, Daniel
AU  - Kupitz, Christopher
AU  - Metz, Markus
AU  - Nelson, Garrett
AU  - Paulraj, Lourdu Xavier
AU  - Beyerlein, Kenneth
AU  - Schmidt, Marius
AU  - Sarrou, Iosifina
AU  - Spence, John C. H.
AU  - Weierstall, Uwe
AU  - White, Thomas
AU  - Yang, Jay-How
AU  - Zhao, Yun
AU  - Liang, Mengning
AU  - Aquila, Andrew
AU  - Hunter, Mark S.
AU  - Robinson, Joseph S.
AU  - Koglin, Jason E.
AU  - Boutet, Sébastien
AU  - Fromme, Petra
AU  - Barty, Anton
AU  - Chapman, Henry N.
TI  - Macromolecular diffractive imaging using imperfect crystals
JO  - Nature 
VL  - 530
IS  - 7589
SN  - 0028-0836
CY  - London [u.a.]
PB  - Nature Publ. Group
M1  - PUBDB-2016-01028
SP  - 202 - 206
PY  - 2016
N1  - (c) Macmillan Publishers Limited
AB  - The three-dimensional structures of macromolecules and their complexes are mainly elucidated by X-ray protein crystallography. A major limitation of this method is access to high-quality crystals, which is necessary to ensure X-ray diffraction extends to sufficiently large scattering angles and hence yields information of sufficiently high resolution with which to solve the crystal structure. The observation that crystals with reduced unit-cell volumes and tighter macromolecular packing often produce higher-resolution Bragg peaks suggests that crystallographic resolution for some macromolecules may be limited not by their heterogeneity, but by a deviation of strict positional ordering of the crystalline lattice. Such displacements of molecules from the ideal lattice give rise to a continuous diffraction pattern that is equal to the incoherent sum of diffraction from rigid individual molecular complexes aligned along several discrete crystallographic orientations and that, consequently, contains more information than Bragg peaks alone. Although such continuous diffraction patterns have long been observed—and are of interest as a source of information about the dynamics of proteins—they have not been used for structure determination. Here we show for crystals of the integral membrane protein complex photosystem II that lattice disorder increases the information content and the resolution of the diffraction pattern well beyond the 4.5 \mathringA limit of measurable Bragg peaks, which allows us to phase the pattern directly. Using the molecular envelope conventionally determined at 4.5 \mathringA as a constraint, we obtain a static image of the photosystem II dimer at a resolution of 3.5 \mathringA. This result shows that continuous diffraction can be used to overcome what have long been supposed to be the resolution limits of macromolecular crystallography, using a method that exploits commonly encountered imperfect crystals and enables model-free phasing.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000369916700035
C6  - pmid:26863980
DO  - DOI:10.1038/nature16949
UR  - https://bib-pubdb1.desy.de/record/294153
ER  -