Matthew G. Iadanza, Ph.D.
Affiliations: | 2014 | Biochemistry | University of Washington, Seattle, Seattle, WA |
Area:
cryoEM of membrane proteinsGoogle:
"Matthew Iadanza"Mean distance: 19.48 (cluster 11)
Parents
Sign in to add mentor| Tamir Gonen | grad student | 2014 | University of Washington | |
| (Protein structure determination by electron diffraction of 3-dimensional protein microcrystals.) | ||||
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Publications
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| Gallardo R, Iadanza MG, Xu Y, et al. (2020) Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly. Nature Structural & Molecular Biology |
| Kontziampasis D, Klebl DP, Iadanza MG, et al. (2019) A cryo-EM grid preparation device for time-resolved structural studies. Iucrj. 6: 1024-1031 |
| Thompson RF, Iadanza MG, Hesketh EL, et al. (2018) Collection, pre-processing and on-the-fly analysis of data for high-resolution, single-particle cryo-electron microscopy. Nature Protocols |
| Iadanza MG, Jackson MP, Hewitt EW, et al. (2018) A new era for understanding amyloid structures and disease. Nature Reviews. Molecular Cell Biology |
| Iadanza MG, Silvers R, Boardman J, et al. (2018) The structure of a beta2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nature Communications. 9: 4517-4517 |
| Iadanza MG, Higgins AJ, Schiffrin B, et al. (2016) Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM. Nature Communications. 7: 12865 |
| Iadanza MG, Jackson MP, Radford SE, et al. (2016) MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images. Scientific Reports. 6: 21078 |
| Rawson S, Iadanza MG, Ranson NA, et al. (2016) Methods to account for movement and flexibility in cryo-EM data processing Methods. 100: 35-41 |
| Wisedchaisri G, Park MS, Iadanza MG, et al. (2014) Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE. Nature Communications. 5: 4521 |
| Iadanza MG, Gonen T. (2014) A suite of software for processing MicroED data of extremely small protein crystals. Journal of Applied Crystallography. 47: 1140-1145 |