Papers
5
Total Citations
304
H-Index
4
About
Mitchell D. Miller is a structural biologist and crystallographic methods developer whose work has significantly advanced the technical infrastructure of modern protein crystallography. Based at the Stanford Synchrotron Radiation Laboratory (SSRL), Miller has made landmark contributions to the automation of X-ray crystallography, most notably through the development of a robotic system for mounting cryo-cooled protein crystals on synchrotron beamlines. This pioneering work, published in 2002 and amassing over 260 citations, introduced compact cassette-based sample handling that transformed high-throughput structural biology workflows worldwide. Complementing this, his 2005 paper on infrared imaging techniques for locating crystals in cryoloops offered an elegant practical solution to a persistent experimental challenge. Beyond instrumentation, Miller has contributed to structural genomics through high-resolution crystal structure determinations of enzymes from the thermophilic organism *Thermotoga maritima*, including γ-glutamyl phosphate reductase and uronate isomerase, shedding light on metabolic pathways in extremophiles. His combined focus on methodology and structural discovery makes him a foundational figure in the modernization of synchrotron-based crystallography infrastructure.
Research Focus
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