Martin Vink

New York Structural Biology Center, Icahn School of Medicine at Mount Sinai

Papers

Total Citations

105

H-Index

About

Martin Vink is a structural biologist whose research has made significant contributions to the field of membrane protein crystallography, with a particular focus on developing high-throughput and automated methodologies for two-dimensional crystallization. His work addresses one of the most persistent challenges in structural biology — obtaining well-ordered crystals of membrane proteins, which are notoriously difficult to crystallize due to their hydrophobic nature and instability outside lipid environments. Vink's most influential contribution, published in 2007 and accumulating 44 citations, introduced a high-throughput screening strategy that dramatically accelerated the identification of optimal conditions for 2D crystallization of membrane proteins. Building on this foundation, his 2010 studies further advanced the field by integrating automated electron microscopy into the crystallization evaluation pipeline, together garnering over 60 additional citations. These tools transformed what was once a laborious, trial-and-error process into a streamlined, reproducible workflow accessible to the broader structural biology community. By combining automation with electron microscopy, Vink's work has enabled researchers to systematically and efficiently pursue membrane protein structures, ultimately supporting drug discovery efforts and deepening our understanding of cellular transport and signaling mechanisms.