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Yilmaz Alguel

Researcher at Imperial College London

Publications -  19
Citations -  1157

Yilmaz Alguel is an academic researcher from Imperial College London. The author has contributed to research in topics: Membrane protein & Efflux. The author has an hindex of 12, co-authored 19 publications receiving 993 citations. Previous affiliations of Yilmaz Alguel include Rutherford Appleton Laboratory.

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Journal ArticleDOI

Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography

TL;DR: A systematic approach to the scaling and merging of data from multiple crystals in macromolecular crystallography is introduced and explained.
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Crystal structure of the anion exchanger domain of human erythrocyte band 3

TL;DR: The crystal structure of the transmembrane anion exchanger domain of AE1 is reported, which includes 14 trans Membrane helices and provides a basis for understanding the effects of mutations that lead to red blood cell diseases and also gives insight into the mechanism of ion transport.
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Benchmarking Membrane Protein Detergent Stability for Improving Throughput of High-Resolution X-ray Structures

TL;DR: It is suggested that by monitoring membrane protein stability with reference to the benchmarks described here, greater efforts can be placed on constructs and conditions more likely to yield high-resolution structures.
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Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context.

TL;DR: The crystal structure of the dimeric membrane domain of human Band 3(1), the red cell chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1), provides a structural context for over four decades of studies into this historic and important membrane glycoprotein.
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Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials.

TL;DR: Five high-resolution crystal structures of TtgR from the solvent-tolerant strain DOT-T1E are reported, including T TGR in complex with common antibiotics and plant secondary metabolites, which provides structural basis for the unique ligand binding properties of TTGR.