Xuemei Li

Institute of physics china, Peping, Beijing, China

Are you Xuemei Li?

Claim your profile

Publications (120)556.13 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: The cyclic nucleotide-binding (CNB)-like protein (CNB-L) from Brucella abortus shares sequence homology with CNB domain-containing proteins. We determined the crystal structure of CNB-L at 2.0-Å resolution in the absence of its C-terminal helix and nucleotide. The 3D structure of CNB-L is in a two-fold symmetric form. Each protomer shows high structure similarity to that of cGMP-binding domain-containing proteins, and likely mimics their nucleotide-free conformation. A key residue, Glu17, mediates the dimerization and prevents binding of cNMP to the canonical ligand-pocket. The structurally observed dimer of CNB-L is stable in solution, and thus is likely to be biologically relevant.
    No preview · Article · Nov 2015 · Biochemical and Biophysical Research Communications
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Shiga-like toxins (Stxs) produced by pathogenic Escherichia coli are a major virulence factor involved in severe diseases in human and animals. These toxins are ribosome-inactivating proteins and treatment for diseases caused by them is not available. So there is an urgent need for agents capable of effectively targeting this lethal toxin. In this paper, we identified baicalin, a flavonoid compound from Chinese traditional medicine as a compound against Shiga-like toxin 2 (Stx2). We found that baicalin significantly improves the renal function and reduces Stx2-induced lethality in mice. Further experiments reveal that baicalin induces the formation of oligomers by the toxin by direct binding. We also identified the residues important for such interactions and have analyzed their roles in binding baicalin by biophysical and biochemical analyses. Our results establish baicalin as a candidate compound for the development of therapeutics against diseases caused by Stxs.
    Full-text · Article · Sep 2015 · Antimicrobial Agents and Chemotherapy
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Importance: Hand-foot-and-mouth disease is a serious public health threat to children in Asian-Pacific countries, resulting in millions of cases. EV71 and CVA16 are the two dominant causative agents of a disease that, whilst usually mild, can cause severe neurological complications, leading to hundreds of deaths. EV71 vaccines do not provide protection against CVA16. A CVA16 vaccine or bivalent EV71/CVA16 vaccine is therefore urgently needed. We report atomic structures for the mature CVA16 virus, natural empty particles, and a recombinant CVA16 virus-like particle that does not contain the viral genome. All three particles have similar structures and identical antigenicity. The recombinant particles produced in insect cells (a system suitable for making vaccine antigen) are stabilised by recruiting from the insect cells a small molecule different to that used by the virus in a normal infection. We present structural and immunogenic comparisons with EV71 to facilitate structure-based drug-design and vaccine development.
    Full-text · Article · Aug 2015 · Journal of Virology
  • Source
    Wu Liu · Yutao Chen · Xi Jiang · Ming Xia · Yang Yang · Ming Tan · Xuemei Li · Zihe Rao
    [Show abstract] [Hide abstract]
    ABSTRACT: Norovirus (NoV) causes epidemic acute gastroenteritis in humans, whereby histo-blood group antigens (HBGAs) play an important role in host susceptibility. Each of the two major genogroups (GI and GII) of human NoVs recognizes a unique set of HBGAs through a distinct binding interface that is conserved within a genogroup, indicating a distinct evolutionary path for each genogroup. Here, we characterize a Lewis a (Lea) antigen binding strain (OIF virus) in the GII.21 genotype that does not share the conserved GII binding interface, revealing a new evolution lineage with a distinct HBGA binding interface. Sequence alignment showed that the major residues contributing to the new HBGA binding interface are conserved among most members of the GII.21, as well as a closely related GII.13 genotype. In addition, we found that glycerol inhibits OIF binding to HBGAs, potentially allowing production of cheap antivirals against human NoVs. Taken together, our results reveal a new evolutionary lineage of NoVs selected by HBGAs, a finding that is important for understanding the diversity and widespread nature of NoVs.
    Full-text · Article · Jul 2015 · PLoS Pathogens
  • Yu Dong · Jun Li · Xiaodi Qiu · Chuanqiang Yan · Xuemei Li
    [Show abstract] [Hide abstract]
    ABSTRACT: The (3R)-hydroxyacyl-ACP dehydratase HadAB, involved in the biosynthetic pathway for mycolic acid (MA) of Mycobacterium tuberculosis, catalyzes the third step in the fatty acid (FA) elongation cycle, which is an ideal and actual target for anti-tubercular agent. Though HadAB is predicted to be a member of the hotdog superfamily, it shares no sequence identity with typical hotdog fold isoenzyme FabZ. To characterize the significance of HadAB from the perspective of structural biology, large amount of pure HadAB complex is required for biochemical characterization and crystallization. Here, we used a unique expression and purification method. HadA and HadB were cloned separately and co-expressed in Escherichia coli. After GST affinity chromatography, two steps of anion exchange chromatography and gel filtration, the purity of the protein as estimated by SDS-PAGE was >95%. Using hanging-drop vapor-diffusion method, crystals were obtained and diffracted X-rays to 1.75Å resolution. The crystal belongs to space group P41212, with unit-cell parameters a=b=82.0Å, c=139.8Å, α=β=γ=90.0°. Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.
    No preview · Article · Jun 2015 · Protein Expression and Purification
  • Source
    Yu Dong · Xiaodi Qiu · Neil Shaw · Yueyang Xu · Yuna Sun · Xuemei Li · Jun Li · Zihe Rao
    [Show abstract] [Hide abstract]
    ABSTRACT: Dehydration is one of the key steps in the biosynthesis of mycolic acids and is vital to the growth of Mycobacterium tuberculosis (Mtb). Consequently, stalling dehydration cures tuberculosis (TB). Clinically used anti-TB drugs like thiacetazone (TAC) and isoxyl (ISO) as well as flavonoids inhibit the enzyme activity of the β-hydroxyacyl-ACP dehydratase HadAB complex. How this inhibition is exerted, has remained an enigma for years. Here, we describe the first crystal structures of the MtbHadAB complex bound with flavonoid inhibitor butein, 2’,4,4’-trihydroxychalcone or fisetin. Despite sharing no sequence identity from Blast, HadA and HadB adopt a very similar hotdog fold. HadA forms a tight dimer with HadB in which the proteins are sitting side-by-side, but are oriented anti-parallel. While HadB contributes the catalytically critical His-Asp dyad, HadA binds the fatty acid substrate in a long channel. The atypical double hotdog fold with a single active site formed by MtbHadAB gives rise to a long, narrow cavity that vertically traverses the fatty acid binding channel. At the base of this cavity lies Cys61, which upon mutation to Ser confers drug-resistance in TB patients. We show that inhibitors bind in this cavity and protrude into the substrate binding channel. Thus, inhibitors of MtbHadAB exert their effect by occluding substrate from the active site. The unveiling of this mechanism of inhibition paves the way for accelerating development of next generation of anti-TB drugs. Electronic supplementary material The online version of this article (doi:10.1007/s13238-015-0181-1) contains supplementary material, which is available to authorized users.
    Full-text · Article · Jun 2015 · Protein & Cell
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Toxic ribosome-inactivating proteins (RIPs) abolish cell viability by inhibiting protein synthesis. Ricin, a member of these lethal proteins, is a potential bioterrorism agent. Despite the grave challenge posed by these toxins to public health, post-exposure treatment for intoxication caused by these agents currently is unavailable. In this study, we report the identification of baicalin extracted from Chinese herb medicine as a compound capable of inhibiting the activity of ricin. More importantly, post-exposure treatment with baicalin significantly increased the survival of mice poisoned by ricin. We determined the mechanism of action of baicalin by solving the crystal structure of its complex with the A chain of ricin (RTA) at a 2.2 Å resolution, which revealed that baicalin interacts with two RTA molecules at a novel binding site by hydrogen bond networks and electrostatic force interactions, suggesting its role as molecular glue of the RTA. Further biochemical and biophysical analyses validated the amino acids directly involved in binding the inhibitor, which is consistent with the hypothesis that baicalin exerts its inhibitory effects by inducing RTA to form oligomers in solution, a mechanism that is distinctly different from previously reported inhibitors. This work offers promising leads for the development of therapeutics against ricin and probably other RIPs. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Full-text · Article · Apr 2015 · Journal of Biological Chemistry
  • Xuemei Li · Linlin Wang · Chunxiang Li
    [Show abstract] [Hide abstract]
    ABSTRACT: An ultrasensitive surface-enhanced Raman spectroscopy (SERS) sensor based on rolling-circle amplification (RCA)-increased "hot-spot" was developed for the detection of thrombin. The sensor contains a SERS gold nanoparticle@Raman label@SiO2 core-shell nanoparticle probe in which the Raman reporter molecules are sandwiched between a gold nanoparticle core and a thin silica shell by a layer-by-layer method. Thrombin aptamer sequences were immobilized onto the magnetic beads (MBs) through hybridization with their complementary strand. In the presence of thrombin, the aptamer sequence was released; this allowed the remaining single-stranded DNA (ssDNA) to act as primer and initiate in situ RCA reaction to produce long ssDNAs. Then, a large number of SERS probes were attached on the long ssDNA templates, causing thousands of SERS probes to be involved in each biomolecular recognition event. This SERS method achieved the detection of thrombin in the range from 1.0×10(-12) to 1.0×10(-8) M and a detection limit of 4.2×10(-13) M, and showed good performance in real serum samples. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
    No preview · Article · Mar 2015 · Chemistry - A European Journal
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Human noroviruses (huNoVs) recognize histo-blood group antigens (HBGAs) as attachment factors, in which genogroup (G) I and GII huNoVs use distinct binding interfaces. The genetic and evolutionary relationships of GII huNoVs under selection by the host HBGAs have been well elucidated via a number of structural studies; however, such relationships among GI NoVs remain less clear due to the fact that the structures of HBGA-binding interfaces of only three GI NoVs with similar binding profiles are known. In this study the crystal structures of the P dimers of a Lewis-binding strain, the GI.8 Boxer virus (BV) that does not bind the A and H antigens, in complex with the Lewis b (Le(b)) and Le(y) antigens, respectively, were determined and compared with those of the three previously known GI huNoVs, i.e. GI.1 Norwalk virus (NV), GI.2 FUV258 (FUV) and GI.7 TCH060 (TCH) that bind the A/H/Le antigens. The HBGA binding interface of BV is composed of a conserved central binding pocket (CBP) that interacts with the β-galactose of the precursor, and a well-developed Le epitope-binding site formed by five amino acids, including three consecutive residues from the long P-loop and one from the S-loop of the P1 subdomain, a feature that was not seen in the other GI NoVs. On the other hand, the H epitope/acetamido binding site observed in the other GI NoVs is greatly degenerated in BV. These data explain the evolutionary path of GI NoVs selected by the polymorphic human HBGAs. While the CBP is conserved, the regions surrounding the CBP are flexible, providing freedom for changes. The loss or degeneration of the H epitope/acetamido binding site and the reinforcement of the Le binding site of the GI.8 BV is a typical example of such change selected by the host Lewis epitope.
    Full-text · Article · Dec 2014 · Protein & Cell
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Effect of rearing temperature on growth and thermal tolerance of Schizothorax (Racoma) kozlovi Nikolsky larvae and juveniles was investigated. The fish (start at 12 days post hatch) were reared for nearly 6 months at five constant temperatures of 10, 14, 18, 22 and 26 °C. Then juvenile fish being acclimated at three temperatures of 14, 18 and 22 °C were chosen to determine their critical thermal maximum (CTMax) and lethal thermal maximum (LTMax) by using the dynamic method. Growth rate of S. kozlovi larvae and juveniles was significantly influenced by temperature and fish size, exhibiting an increase with increased rearing temperature, but a decline with increased fish size. A significant ontogenetic variation in the optimal temperatures for maximum growth were estimated to be 24.7 °C and 20.6 °C for larvae and juveniles of S. kozlovi, respectively. The results also demonstrated that acclimation temperature had marked effects on their CTMax and LTMax, which ranged from 32.86 °C to 34.54 °C and from 33.79 °C to 34.80 °C, respectively. It is suggested that rearing temperature must never rise above 32 °C for its successful aquaculture. Significant temperature effects on the growth rate and thermal tolerance both exhibit a plasticity pattern. Determination of critical heat tolerance and optima temperature for maximum growth of S. kozlovi is of ecological significance in the conservation and aquaculture of this species.
    Full-text · Article · Dec 2014 · Journal of Thermal Biology
  • [Show abstract] [Hide abstract]
    ABSTRACT: Hepatitis A virus (HAV) remains enigmatic, despite 1.4 million cases worldwide annually. It differs radically from other picornaviruses, existing in an enveloped form and being unusually stable, both genetically and physically, but has proved difficult to study. Here we report high-resolution X-ray structures for the mature virus and the empty particle. The structures of the two particles are indistinguishable, apart from some disorder on the inside of the empty particle. The full virus contains the small viral protein VP4, whereas the empty particle harbours only the uncleaved precursor, VP0. The smooth particle surface is devoid of depressions that might correspond to receptor-binding sites. Peptide scanning data extend the previously reported VP3 antigenic site, while structure-based predictions suggest further epitopes. HAV contains no pocket factor and can withstand remarkably high temperature and low pH, and empty particles are even more robust than full particles. The virus probably uncoats via a novel mechanism, being assembled differently to other picornaviruses. It utilizes a VP2 'domain swap' characteristic of insect picorna-like viruses, and structure-based phylogenetic analysis places HAV between typical picornaviruses and the insect viruses. The enigmatic properties of HAV may reflect its position as a link between 'modern' picornaviruses and the more 'primitive' precursor insect viruses; for instance, HAV retains the ability to move from cell-to-cell by transcytosis.
    No preview · Article · Oct 2014 · Nature
  • Source

    Full-text · Dataset · Oct 2014
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Mycobacterium tuberculosis (Mtb) uses maltose-1-phosphate to synthesize α-glucans that make up the major component of its outer capsular layer. Maltose kinase (MaK) catalyzes phosphorylation of maltose. The molecular basis for this phosphorylation is currently not understood. Here, we describe the first crystal structure of MtbMaK refined to 2.4 Å resolution. The bi-modular architecture of MtbMaK reveals a remarkably unique N-lobe. An extended sheet protrudes into ligand binding pocket of an adjacent monomer and contributes residues critical for kinase activity. Structure of the complex of MtbMaK bound with maltose reveals that maltose binds in a shallow cavity of the C-lobe. Structural constraints permit phosphorylation of α-maltose only. Surprisingly, instead of a Gly-rich loop, MtbMaK employs 'EQS' loop to tether ATP. Notably, this loop is conserved across all MaK homologues. Structures of MtbMaK presented here unveil features that are markedly different from other kinases and support the scaffolding role proposed for this kinase.
    Preview · Article · Sep 2014 · Scientific Reports
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: AimsA study was conducted to compare the intestinal microbial compositions of two fish species with similar feeding strategy; paddlefish (Polyodon spathala) and bighead carp (Aristichthys nobilis) reared in the same pond. Methods and ResultsAge-0 paddlefish and bighead carp with mean average body lengths of 4339278 and 1933368cm, respectively, were reared with natural prey items in the same pond (20m(2)). After 30days of rearing, the intestinal microbiota of the two fish species was assessed by pyrosequencing of 16S rRNA genes. Interestingly, deviations were observed in the microbial communities of the two fish species according to the alpha- and beta-diversity measurements and detrended correspondence analysis (DCA). Shannon diversity (P=0015) and Pielou.evenness (P=0035) revealed significant lower diversity of the intestinal microbiota of paddlefish. Moreover, different core intestinal microbiota was noticed in the two fish species. Proteobacteria (573%), Firmicutes (119%), Fusobacteria (89%), Planctomycetes (73%), Actinobacteria (60%) and Verrucomicrobia (32%) were detected in bighead carp, while the dominant phyla in paddlefish intestines were Bacteroidetes (370%), Fusobacteria (351%), Firmicutes (148%) and Proteobacteria (126%). Conclusions Our results revealed that the intestinal microbiota differed between paddlefish and bighead carp reared in the same pond when fed similar nature food. The potential host factors, such as the genetic background, gut histology and physiology are assumed to be involved in the intestinal bacterial compositions. Significance and Impact of the StudyConsidering the similar feeding strategy of paddlefish and bighead carp, this study presents basic knowledge for evaluation of the importance of host factors (genetic background and gut anatomy) on intestinal microbial composition.
    Full-text · Article · Aug 2014 · Journal of Applied Microbiology
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Unlike the well-established picture for the entry of enveloped viruses, the mechanism of cellular entry of non-enveloped eukaryotic viruses remains largely mysterious. Picornaviruses are representative models for such viruses, and initiate this entry process by their functional receptors. Here we present the structural and functional studies of SCARB2, a functional receptor of the important human enterovirus 71 (EV71). SCARB2 is responsible for attachment as well as uncoating of EV71. Differences in the structures of SCARB2 under neutral and acidic conditions reveal that SCARB2 undergoes a pivotal pH-dependent conformational change which opens a lipid-transfer tunnel to mediate the expulsion of a hydrophobic pocket factor from the virion, a pre-requisite for uncoating. We have also identified the key residues essential for attachment to SCARB2, identifying the canyon region of EV71 as mediating the receptor interaction. Together these results provide a clear understanding of cellular attachment and initiation of uncoating for enteroviruses. Electronic supplementary material The online version of this article (doi:10.1007/s13238-014-0087-3) contains supplementary material, which is available to authorized users.
    Full-text · Article · Jul 2014 · Protein & Cell
  • Xiaotao Guan · Jun Li · Xingru Lü · Yu Dong · Weimin Chen · Xuemei Li
    [Show abstract] [Hide abstract]
    ABSTRACT: The tripartite motif-containing protein 2 (TRIM2) functions as an E3 ubiquitin ligase. Loss of function of TRIM2 has been shown to result in early-onset axonal neuropathy. As a member of the TRIM-NHL family of proteins, TRIM2 has a conserved modular architecture that includes N-terminal RING finger and B-box domains, a middle coiled-coil domain and a C-terminal NHL domain. To characterize the functional role of its NHL domain from the perspective of structural biology, a truncation of human TRIM2 (residues 465-744) was expressed, purified and crystallized. Rod-shaped crystals were obtained that diffracted X-rays to 1.7 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 43.6, b = 76.4, c = 107.4 Å, α = 90.0, β = 94.0, γ = 90.0°. A Matthews coefficient of 1.97 Å(3) Da(-1), corresponding to a solvent content of 37.6%, indicated the presence of three molecules per asymmetric unit, which was further confirmed by the phasing solution from molecular replacement.
    No preview · Article · May 2014 · Acta Crystallographica Section F: Structural Biology Communications
  • Xuemei Li · Yan Wang · Linlin Wang · Qingli Wei
    [Show abstract] [Hide abstract]
    ABSTRACT: A surface plasmon resonance (SPR) detection system based on a hybridization chain reaction (HCR) was developed for amplified detection of DNA and small molecule with high sensitivity.
    No preview · Article · Apr 2014 · Chemical Communications
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The prokaryotic 5'-Methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH), a process that plays a key role in several metabolic pathways. Its absence in all mammalian species has implicated this enzyme as a promising target for antimicrobial drug design. Here, we report the crystal structure of BmMTAN in complex with its product adenine at a resolution of 2.6 Å determined by single-wavelength anomalous dispersion method. 11 key residues were mutated for kinetic characterization. Mutations of Tyr134 and Met144 resulted in the largest overall increase in Km, whereas mutagenesis of residues Glu18, Glu145 and Asp168 completely abolished activity. Glu145 and Asp168 were identified as active site residues essential for catalysis. The catalytic mechanism and implications of this structure for broad-based antibiotic design are discussed.
    Preview · Article · Mar 2014 · Biochemical and Biophysical Research Communications
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Enterovirus 71 (HEV71) epidemics in children and infants result mainly in mild symptoms; however, especially in the Asia-Pacific region, infection can be fatal. At present, no therapies are available. We have used structural analysis of the complete virus to guide the design of HEV71 inhibitors. Analysis of complexes with four 3-(4-pyridyl)-2-imidazolidinone derivatives with varying anti-HEV71 activities pinpointed key structure-activity correlates. We then identified additional potentially beneficial substitutions, developed methods to reliably triage compounds by quantum mechanics-enhanced ligand docking and synthesized two candidates. Structural analysis and in vitro assays confirmed the predicted binding modes and their ability to block viral infection. One ligand (with IC50 of 25 pM) is an order of magnitude more potent than the best previously reported inhibitor and is also more soluble. Our approach may be useful in the design of effective drugs for enterovirus infections.
    Full-text · Article · Feb 2014 · Nature Structural & Molecular Biology
  • Xuemei Li · Jian Song · Yan Wang · Tao Cheng
    [Show abstract] [Hide abstract]
    ABSTRACT: A structure-switching-based approach for the design of fluorescent biosensors from known RNA aptazymes were demonstrated for the detection of theophylline and thiamine pyrophosphate (TPP). Taking advantages of the ability of graphene oxide (GO) to protect ssDNA from nuclease cleavage and the cyclic amplification induced by deoxyribonuclease I (DNase I), the amplified assay showed high sensitivity. In the presence of target, the target-dependent hammerhead aptazyme cleaves off. The released Shine-Dalgarno (SD) sequence was introduced into the detection system, in which a FAM labeled probe ssDNA was noncovalently assembled on GO, and the fluorescence of the dye was completely quenched. In the presence of the released sequence, the binding between the dye-labeled DNA and the SD sequence alter the conformation of dye-labeled DNA, and disturb the interaction between the dye-labeled DNA and GO, liberating dye-labeled DNA from GO. The fluorescent intensity was increased, whereupon the DNase I can cleave the free DNA in the DNA/RNA complex, thereby liberating the fluorophore and ultimately releasing the SD RNA sequence. The released SD RNA sequence then binds another DNA probe, and the cycle starts anew, which leads to significant amplification of the fluorescent signal. The strategy showed good sensitivity and the dynamic ranges were of 0.1-10μM and 0.5-100μM for theophylline and TPP, respectively. The approach opens up a wide range of possibilities for sensing of other small molecules in biological entities.
    No preview · Article · Oct 2013 · Analytica chimica acta

Publication Stats

3k Citations
556.13 Total Impact Points


  • 2015
    • Institute of physics china
      Peping, Beijing, China
  • 2013-2015
    • Linyi University
      Yichow, Shandong Sheng, China
    • Huazhong University of Science and Technology
      • School of Environmental Science and Engineering
      Wu-han-shih, Hubei, China
  • 2003-2015
    • Chinese Academy of Sciences
      • • National Laboratory of Biomacromolecules
      • • Graduate School
      • • Institute of Biophysics
      • • Institute of Hydrobiology
      • • State Key Laboratory of Reproductive Biology
      • • Institute of Zoology
      Peping, Beijing, China
  • 2014
    • University of Cincinnati
      • Department of Pediatrics
      Cincinnati, Ohio, United States
    • Chinese Academy of Fishery Sciences
      Peping, Beijing, China
  • 2013-2014
    • Chinese Academy of Fishery Sciences
      北江, Zhejiang Sheng, China
  • 2009-2013
    • Third Military Medical University
      Ch’ung-ch’ing-shih, Chongqing Shi, China
    • Southwest University in Chongqing
      Pehpei, Chongqing Shi, China
  • 2007-2012
    • Qingdao University of Science and Technology
      Tsingtao, Shandong Sheng, China
  • 2010-2011
    • Yunnan Academy of Agricultural Sciences
      Yün-nan, Yunnan, China
    • Nankai University
      • College of Life Sciences
      T’ien-ching-shih, Tianjin Shi, China
  • 2004-2009
    • Tsinghua University
      • Laboratory of Structural Biology
      Peping, Beijing, China
    • National Tsing Hua University
      Hsin-chu-hsien, Taiwan, Taiwan
  • 2008
    • Yunnan University
      • Laboratory for Conservation and Utilization of Bio-resources
      Yün-nan, Yunnan, China
    • China Agricultural University
      • Department of Biochemistry and Molecular Biology
      Peping, Beijing, China