Supplementary Figure 1: X-ray and corresponding MicroED diffraction pattern from protein tau.
From: Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED
(Left) When extracted from hanging drops, a cluster of microneedle crystals of the amyloid-forming protein tau diffracts as powder to no better than 4.2 Å using a rotating anode X-ray source. Physically breaking these needle clusters and selecting individual sub-micron thick crystal fragments yields diffraction to atomic resolution by MicroED (right) and a structure solvable by direct methods. The X-ray diffraction pattern was collected over a 6° oscillation range; the MicroED pattern spans a 0.6° wedge. See main text for data collection details.
