Modular Construction on a Biomolecular Scale

The spherical protein ferritin was used to synthesize a porous 3-D crystalline framework material, and further engineered to have metal hubs on its surface.  Organic molecules bridge these hubs, and in a controlled way create a porous material with potential uses from efficient fuel storage to carbon capture and conversion.  The study shows the great potential for proteins as building blocks with exquisite properties of electron transfer and bioinspired catalysis.

A. Sontz, J. B. Bailey, S. Ahn and F. A. Tezcan, “A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals”, J. Am. Chem. Soc. 137, 11598 (2015), doi: 10.1021/jacs.5b07463

Funding Acknowledgements: Work supported by the Office of Basic Energy Sciences (OBES) Division of Materials Sciences, U.S. Department of Energy (DOE) Office of Science, Award DE-FG02-10ER46677 to F.A.T. Crystallographic data collected at Stanford Synchrotron Radiation Laboratory (SSRL), SLAC National Accelerator Laboratory (SLAC), supported by two DOE offices: OBES and OBER, as well as by the National Institutes of Health (NIH). Coordinate and structure factor files deposited into Protein Data Bank under accession numbers 5CMQ and 5CMR.

Protein Cage

Using Small-angle X-ray scattering (SAXS) to efficiently and quickly image large protein molecular assemblies, scientists have designed a hollow, cube-shaped protein cage that has the potential for delivering proteins or other chemicals to specific locations for medical, energy, and other applications. The nanocage crystal structure was optimized at the Advanced Light Source (Image courtesy of Greg Hura, LBNL).

Lai, Y.T., E. Reading, G.L. Hura, K.L.Tsai, A. Laganowsky, F.J. Asturias,  J.A. Tainer, C.V. Robinson, and T.O. Yeates. 2014.“Structure of a Designed Protein Cage that Self-Assembles into a Highly Porous Cube,” Nature Chemistry 6, 1065–1071. doi:10.1038/nchem.2107

Feature Article at LBNL

Funding Acknowledgements: Work supported by National Science Foundation (NSF; grant CHE-1332907, T.O.Y.), Office of Biological and Environmental Research (OBER), U.S. Department of Energy (DOE) Office of Science, and the National Institutes of Health (NIH; grant R01GM067167, F.J.A.). SAXS data collection and analysis at BL12.3.1 at the Advanced Light Source (ALS), Lawrence Berkeley National Laboratory (LBNL) supported by the Integrated Diffraction Analysis Technologies (IDAT) program (DOE OBER), by DOE (contract DE-AC02-05CH11231) and by NIH Minocycline to Improve Neurologic Outcome in Stroke (MINOS; R01GM105404).

X-rays and Protein Crystal Samples

Lessening X-ray damage is healthy for protein discovery data too

Image credit: Wayne Anderson, Northwestern University.

Protein crystal samples are placed on a small metal tip so x-rays from the adjacent beam pipe can pass through them and diffract off the atoms inside the crystal. Using computational methods, scientists interpret the scattered light patterns recorded by detectors to create an image of how the atoms are located inside the crystal.

ANL Article

Karolina Michalska, Kemin Tan, Hui Li, Catherine Hatzos-Skintges, Jessica Bearden, Gyorgy Babnigg, and Andrzej Joachimiak. “GH1-family 6-P-β-glucosidases from human microbiome lactic acid bacteria”Acta Cryst. (2013). D69, 451-463. DOI: 10.1107/s0907444912049608

Funding Acknowledgements: Midwest Center for Structural Genomics (MCSG) and Structural Biology Center (SBC) at Argonne National Laboratory (ANL): support. Funding in part: grant from National Institutes of Health (NIH; GM094585) and by the Office of Biological and Environmental Research (OBER), U.S. Department of Energy (DOE) Office of Science, under Contract DE-AC02-06CH11357. Submitted manuscript created by University of Chicago Argonne, LLC, operator of ANL, a DOE Office of Science Laboratory, is operated under Contract No. DE-AC02-06CH11357.