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Can Xie

Can Xie, PhD

Professor of Biophysics

High Magnetic Field Laboratory

Hefei Institutes of Physical Science

Chinese Academy of Sciences 

Science Island, Hefei, China 230031


Adjunct Professor

Beijing Computational Science Research Center (CSRC),

Chinese Academy of Engineering Physics (CAEP)

Formerly: Principal Investigator

Laboratory of Molecular Biophysics 

School of Life Sciences

Peking University


Office: +86-10-62753901

Mobile: +86-18600081469


Dr. Can Xie received his B.A. in Biology with Prof. Youhui Shen from Hunan Normal University in 1995, his Ph.D. in Molecular Genetics and Biochemistry with Prof. Shouyi Chen and Prof. Jinsong Zhang from Institute of Genetics and Developmental Biology, Chinese Academy of Sciences in 2001. He did a fellowship with Dr. Timothy Springer in Harvard Medical School in Boston, USA. He began as Principal Investigator at Peking University (PKU) in 2009 and continued to steer his research program with his impeccable taste of Biology, with two major research fields that connect the disciplines of biology and physics: (I) The molecular mechanism of animal magnetoreception, migration and navigationwith a focus on how do animals sense the geomagnetic field.  (II) Structural color and dynamic color change with a focus on how do octopuses change color. After ten years at Peking University, he decided to move his lab to the Science Island at Hefei in 2019, and has been here ever since. It was somewhat like a bird, probably attracted by the fancy magnets in High Magnetic Field Laboratory of Chinese Academy of Sciences.  He currently is Professor of Biophysics at Hefei Institutes of Physical Science, Chinese Academy of Sciences (CAS) and Adjunct Professor at Beijing Computational Science Research Center (CSRC), Chinese Academy of Engineering Physics (CAEP).

Dr. Xie and his lab have made significant contributions to the field of animal magnetoreception and navigation by identifying the world’s first putative magnetoreceptor (MagR, Qin et al. 2016, Nature Materials), a protein with innate magnetic feature. It was regarded as “opened a new field” and “remarkable discovery”, and has profound influence on both biological and physical fields. This work has been followed up by many other scientists in the world. 

Dr. Xie and his lab are making contributions to the structural coloration and bio-invisibility field as well. Camouflage and warning coloration are used extensively in nature and by humans in some form or another since the beginning of human civilization. We are trying to understand the molecular mechanism of reflectin-mediated dynamic structural coloration and bio-invisibility, and with a perspective for bioinspired photonic materials.

Almost 15 years of research experience on receptor and sensory biology, walking through a long journey from ecology, molecular biology, biochemistry, structural biology and biophysics, Dr. Can Xie made multiple discoveries previously. 


Dr. Xie previously successfully isolated a new transmembrane receptor gene NTHK1 in plant (Nicotiana tabacum histidine kinase-like 1) during his Ph.D with Prof. Shouyi Chen and Jinsong Zhang. He showed that NTHK1 is actually not a Histidine Kinase (HK) as suggested by its high homology to its ancient ancestors in prokaryotes, but a Serine-Threonine Kinase (STK). The findings not only overturned a previously proposed mechanism for ethylene receptor signaling which based on a false prediction that all ethylene receptors are histidine-kinase, but also provided an explanation why there is no HK found in animals whereas STK are wide-spreaded, opposite to the prokaryotes world. The work has been successfully replicated by many labs later on and widely accepted worldwide.

During his postdoc fellowship with Timothy Springer at Harvard, Dr. Xie I determined the electron microscopic (EM) structures of two leukocyte I-domain containing integrins (L2 andX2) for the first time (working with Nori Nishida). Three distinctive conformations were identified and the transition between a bent conformation and two extended conformations was suggested as a universal mechanism for integrin activation. Integrin aXb2 has every unfavorable features haunting structural studies, such as high molecular weight (>200KDa), heterodimer, disulfide-bond, highly glycosylated, sticky (the protein literally binds almost everything including plastic tube, glass, BSA and so on), and extremely flexibility, the crystal diffracted very poorly, and getting the phase remained one of the biggest obstacles for structural determination. Dr. Xie spent eight years and finally solved the long-waiting crystal structure of integrin aXb2, which is also the first crystal structure of complement receptor (working with Jianghai Zhu). The work has been done during this stage by Dr. Xie and other Scientists, explain at the molecular level how immunologically important integrins become activated in the immunological synapse in immune responses, at the leukocyte-endothelial interface in leukocyte trafficking from blood to tissues, and in phagocytosis of opsonized pathogens.


Dr. Can Xie's academic interests now focus on the the molecular mechanism of (I) animal magnetoreception, migration and navigation, (II) structural color, dynamic color change and bio-invisibility. As Dr. Hans Frauenfelder proposed in Physical Biology 2014, ‘Ask not what physics can do for biology—ask what biology can do for physics’, Dr. Xie's lab has been working on the interface between the biological and physical worlds. And he loves it.

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