(1) Developing protein expression and purification technology system: Aiming at the problems of protein expression and purification, the platform has developed a variety of expression vectors and host libraries, and built efficient milligram to gram protein expression and purification technology, which have improved the efficiency of protein expression and purification.

1)A complete expression tool library and expression screening system were established. The vector library containing His, GST, MBP and other solubilizing tags and the host library of various hosts (such as Escherichia coli, yeast, etc.) were built, and the expression conditions were high-throughput screened by using high-efficiency orifice shaking tables and diversified protein sample pretreatment processes, which have improved the success rate and efficiency of protein expression, and the overall soluble expression rate has increased by nearly 80%.

2)A milligram high-throughput protein expression technology system has been established. Through automatic equipment and magnetic-beads purification technology, the purification process was optimized, and the purification of 24 samples can be achieved within 2 hours, which improved the efficiency by more than ten times. The high-throughput culture of up to 9000 samples can be realized at the same time. The pretreatment capacity of 100 uL-4 mL samples can reach 400-1600 samples/day, and the purification ability of milligram samples can reach more than 10 thousand every year, and the purity exceeds 85%.

3)A gram-level high-throughput protein expression and purification technology chain was established. Using parallel fermenters and multiple sets of shaking tables, the fermentation and expression conditions were optimized to realize the large-scale culture of 54 samples in each batch; Through parallel and series automatic purification systems, the whole process from fermentation to purification can be automatically processed, and the preparation efficiency of large-scale samples has been improved. The sample preparation capacity of 100 mg to 1 g or more reaches 300-600 samples/year, and the purity exceeds 95%.

(2) Establishing high-throughput, automatic and standardized protein property determination methods, such as protein stability determination, kinetic determination, etc., screen protein samples with excellent performance efficiently and quickly, which has improved the ability of rapid characterization of protein properties and functions, realized the comprehensive characterization of industrial enzymes, membrane proteins, anaerobic proteins and antibodies.

1)A protein stability detection system including thermal stability detection and kinetic stability detection was established to comprehensively evaluate the physical and chemical stability of proteins in different environments. 144 samples can be screened in one day, and the parameters such as Tm, Tagg, particle size and polydispersity of proteins can be detected. Industrial enzyme mutants with excellent properties can be quickly and accurately screened in one experiment.

2)Based on nanoDSF technology, a high-throughput screening method for the stability of membrane protein detergents was established, and 16 different detergents were screened to determine the proper detergents which can stable the target membrane protein.

Denaturation curves (BCM curves) were superimposed, and the differences of structural thermal stability under various detergent conditions were judged by the temperature corresponding to the turning point

Aggregation curves (SLS266) were superimposed to judge the differences of colloid stability by the temperature corresponding to the abscissa peak value and the scattered light intensity in the ordinate

Determination of sample quality by dynamic light scattering DLS: homogeneity and particle size

3)Through the automatic expression quantitative identification system, automatic qualitative and quantitative identification method of unknown proteins was established, which realized efficient analysis of 24 samples every time. Automatic expression identification and quantitative detection of 50 samples can be finished every day.






4)Through microplate reader, fluorescence detection, chemiluminescence detection and light absorption detection technologies were developed, and quantitative detection methods of industrial proteins and anaerobic enzymes were established, which realized high-precision and automatic quantitative analysis of proteins and formed the detection ability of processing 10,000 samples every year.

5)A high-throughput protein-small molecule interaction detection technology was established to analyze the interaction between protein and small molecule compounds, which realized the high-sensitivity determination of protein-small molecule interaction. Screening samples with high efficiency can accomplish the interaction detections of thousands of samples every day.




(3) The research and analysis platform of anaerobic protein was established: Aiming at extreme anaerobic enzymes, especially nitrogenase or photosynthesis-related enzymes, the research system of anaerobic protein technology was established to realize the expression and preparation of protein and the preparation of structural biological samples under anaerobic conditions. Based on the anaerobic platform, a complete and efficient anaerobic research technology system has been developed, which includes four functional modules: anaerobic bacteria culture, anaerobic protein preparation, anaerobic enzyme crystallization and anaerobic enzyme properties characterization, providing strong technical support for anaerobic protein research.







Expression, Purification and Crystal Screening of Anaerobic Protein




(4) An efficient structural biology research technology platform has been established, from structural biology sample preparation to automatic observation, to data collection, efficient data processing and structural analysis, forming a complete and efficient technical chain. Combined with AI-assisted structural prediction, the structural analysis of biomolecules can be quickly completed.



1)A high-throughput screening and optimization technology system for protein crystallization conditions was established, and a rapid and stable sample preparation technology for soluble proteins, membrane proteins and small molecules was developed. Based on the automatic crystal screening robot, the sample screening ability has been improved to 10,000 conditions/week, and crystal optimization technologies such as seeding, dehydration and in-situ hydrolysis are introduced and optimized, which improves the success rate and efficiency of crystal optimization.



Protein structure analysis supporting by obtaining high quality crystals using seeding method

2)A frozen electron microscope sample preparation platform was established. Based on the rapid frozen electron microscope sample preparation system composed of a rapid frozen electron microscope sample preparation instrument and a high vacuum coating instrument, the negative staining method was optimized, and a rapid and stable frozen electron microscope sample preparation technology was developed, which can quickly screen and obtain samples that meet the requirements. For samples that are difficult to crystallize, a new means of structural biology research was expanded.

3)An automatic data collection and structure analysis platform was set up, and an experimental process for rapid detection and efficient data collection of biological macromolecule and small molecule crystal was established. Combined with cryoelectron microscope, studying the complex structure of super-large molecular weight protein can be achieved. With the help of high-performance structure analysis, the rapid data processing and analysis were realized, and a complete technical service system for diffraction data collection and protein structure analysis was constructed, with the diffraction data collection capacity reaching 300 sets/year. Providing the whole process service of protein structure analysis for many research units, the structural biology platform has obtained hundreds of crystal structures including small molecules and proteins, which provides strong support for basic research and subsequent development and application of proteins.






Participated in publishing papers in recent five years:

[1] Y. Zhu, P. Chen, Q. Dong, Q. Li, D. Liu, T. Liu, W. Liu, Y. Sun, Protein engineering of transaminase facilitating enzyme cascade reaction for the biosynthesis of azasugars, iScience, 27 (2024) 109034.

[2] Z. Zheng, L. Cong, Z. Li, W. Liu, S. You, X. Han, Identification and characterization of a novel polyamide hydrolase, Sheng Wu Gong Cheng Xue Bao, 40 (2024) 3103-3113.

[3] Y. Zhang, Y. Li, Y. Chen, W. Liu, Q. Zhao, J. Feng, P. Yao, Q. Wu, D. Zhu, Manipulating Activity and Chemoselectivity of a Benzaldehyde Lyase for Efficient Synthesis of α-Hydroxymethyl Ketones and One-Pot Enantio-Complementary Conversion to 1,2-Diols, ACS Catalysis, 14 (2024) 9687-9700.

[4] Q. Wang, L. Cong, J. Guo, J. Wang, X. Han, W. Zhang, W. Liu, H. Wei, S. You, Structure‐Guided Engineering of a Short‐Chain Dehydrogenase LfSDR1 for Efficient Biosynthesis of (R)‐9‐(2‐Hydroxypropyl)adenine, the Key Intermediate of Tenofovir, Advanced Synthesis & Catalysis, (2024).

[5] J. Qiao, Y. Fang, Z. Li, J. Li, J. Cai, W. Liu, H. Wang, X. Zhu, X. Zhang, Experimental evolution reveals an effective avenue for d-lactic acid production from glucose-xylose mixtures via enhanced Glk activity and a cAMP-independent CRP mutation, Biotechnol Bioeng, 121 (2024) 3514-3526.

[6] J. Mican, D.s.M.M. Jaradat, W. Liu, G. Weber, S. Mazurenko, U.T. Bornscheuer, J. Damborsky, R. Wei, D. Bednar, Exploring new galaxies: Perspectives on the discovery of novel PET-degrading enzymes, Applied Catalysis B: Environmental, 342 (2024).

[7] Z.-L. Mei, C.-C. Li, X. Han, Y.-C. Tian, S.-H. Li, W. Liu, G. Qu, M.T. Reetz, Z. Sun, J.-A. Ma, F.-G. Zhang, Enzymatic Stereodivergent Access to Fluorinated β-Lactam Pharmacophores via Triple-Parameter Engineered Ketoreductases, ACS Catalysis, 14 (2024) 6358-6368.

[8] J. Li, R. Li, N. Shang, Y. Men, Y. Cai, Y. Zeng, W. Liu, J. Yang, Y. Sun, Enzymatic Synthesis of Novel Terpenoid Glycoside Derivatives Decorated with N-Acetylglucosamine Catalyzed by UGT74AC1, J Agric Food Chem, 72 (2024) 14255-14263.

[9] C. Che, W. Zhang, X. Xu, Z. Zheng, H. Wei, B. Qin, X. Jia, W. Liu, S. You, Structure-based reshaping of a new ketoreductase from Sphingobacterium siyangense SY1 toward alpha-haloacetophenones, Int J Biol Macromol, 277 (2024) 134157.

[10] C.H. Zhou, X. Chen, T. Lv, X. Han, J.H. Feng, W.D. Liu, Q.Q. Wu, D.M. Zhu, Flipping the Substrate Creates a Highly Selective Halohydrin Dehalogenase for the Synthesis of Chiral 4-Aryl-2-oxazolidinones from Readily Available Epoxides, ACS Catal, 13 (2023) 4768-4777.

[11] Y. Zhao, H. Wang, P. Wu, Z. Li, F. Liu, Q. Gu, W. Liu, J. Gao, X. Han, [Engineering the plastic degradation enzyme Ple629 from marine consortium to improve its thermal stability], Sheng Wu Gong Cheng Xue Bao, 39 (2023) 2040-2052.

[12] H.L. Zhang, X. Chen, T. Lv, Q. Li, W.D. Liu, J.H. Feng, X.T. Liu, P.Y. Yao, Q.Q. Wu, D.M. Zhu, Engineering a Carbonyl Reductase to Simultaneously Increase Activity Toward Bulky Ketone and Isopropanol for Dynamic Kinetic Asymmetric Reduction via Enzymatic Hydrogen Transfer, ACS Catal, 13 (2023) 9960-9968.

[13] P. Wu, Z. Li, J. Gao, Y. Zhao, H. Wang, H. Qin, Q. Gu, R. Wei, W. Liu, X. Han, Characterization of a PBAT Degradation Carboxylesterase from Thermobacillus composti KWC4, Catalysts, 13 (2023).

[14] M. Wei, X. Gao, W. Zhang, C. Li, F. Lu, L. Guan, W. Liu, J. Wang, F. Wang, H.M. Qin, Enhanced Thermostability of an l-Rhamnose Isomerase for d-Allose Synthesis by Computation-Based Rational Redesign of Flexible Regions, J Agric Food Chem, 71 (2023) 15713-15722.

[15] H. Qi, T. Wang, H. Li, C. Li, L. Guan, W. Liu, J. Wang, F. Lu, S. Mao, H.M. Qin, Sequence- and Structure-Based Mining of Thermostable D-Allulose 3-Epimerase and Computer-Guided Protein Engineering To Improve Enzyme Activity, J Agric Food Chem, 71 (2023) 18431-18442.

[16] Y. Chen, J. Gao, Y. Zhao, H. Wang, X. Han, J. Zhang, Q. Gu, Y. Hou, W. Liu, [Expression, purification and characterization of a novel bis (hydroxyethyl) terephthalate hydrolase from Hydrogenobacter thermophilus], Sheng Wu Gong Cheng Xue Bao, 39 (2023) 2015-2026.

[17] Z. Li, J. Gao, C. Chen, R. Guo, W. Liu, X. Han, Structure, Function and Transformation of Polyethylene Terephthalate (PET) Plastic Hydrolase, Biological Processing Process, 20 (2022) 374-384.

[18] T. Zhang, P. Liu, H. Wei, X. Sun, Y. Zeng, X. Zhang, Y. Cai, M. Cui, H. Ma, W. Liu, Y. Sun, J. Yang, Protein Engineering of Glucosylglycerol Phosphorylase Facilitating Efficient and Highly Regio- and Stereoselective Glycosylation of Polyols in a Synthetic System, ACS Catal, 12 (2022) 15715-15727.

[19] L. Zhang, X. Zhang, J. Min, B. Liu, J.W. Huang, Y. Yang, W. Liu, L. Dai, Y. Yang, C.C. Chen, R.T. Guo, Structural insights to a bi-functional isoprenyl diphosphate synthase that can catalyze head-to-tail and head-to-middle condensation, Int J Biol Macromol, 214 (2022) 492-499.

[20] W. Zeng, X.Q. Li, Y.Y. Yang, J. Min, J.W. Huang, W.D. Liu, D. Niu, X.C. Yang, X. Han, L.L. Zhang, L.H. Dai, C.C. Chen, R.T. Guo, Substrate-Binding Mode of a Thermophilic PET Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy, ACS Catal, 12 (2022) 3033-3040.

[21] S. Wu, C. Xiang, Y. Zhou, M.S.H. Khan, W. Liu, C.G. Feiler, R. Wei, G. Weber, M. Hohne, U.T. Bornscheuer, A growth selection system for the directed evolution of amine-forming or converting enzymes, Nat Commun, 13 (2022) 7458.

[22] L.J. Wu, J.H. An, X.R. Jing, C.C. Chen, L.H. Dai, Y. Xu, W.D. Liu, R.T. Guo, Y. Nie, Molecular Insights into the Regioselectivity of the Fe(II)/2-Ketoglutarate-Dependent Dioxygenase-Catalyzed C-H Hydroxylation of Amino Acids, ACS Catal, 12 (2022) 11586-11596.

[23] R. Wei, G. von Haugwitz, L. Pfaff, J. Mican, C.P.S. Badenhorst, W. Liu, G. Weber, H.P. Austin, D. Bednar, J. Damborsky, U.T. Bornscheuer, Mechanism-Based Design of Efficient PET Hydrolases, ACS Catal, 12 (2022) 3382-3396.

[24] G. von Haugwitz, X. Han, L. Pfaff, Q. Li, H. Wei, J. Gao, K. Methling, Y. Ao, Y. Brack, J. Mican, C.G. Feiler, M.S. Weiss, D. Bednar, G.J. Palm, M. Lalk, M. Lammers, J. Damborsky, G. Weber, W. Liu, U.T. Bornscheuer, R. Wei, Structural Insights into (Tere)phthalate-Ester Hydrolysis by a Carboxylesterase and Its Role in Promoting PET Depolymerization, ACS Catal, 12 (2022) 15259-15270.

[25] G. Qu, Y. Bi, B. Liu, J. Li, X. Han, W. Liu, Y. Jiang, Z. Qin, Z. Sun, Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline-Induced Loop Engineering Test, Angew Chem Int Ed Engl, 61 (2022) e202110793.

[26] L. Pfaff, J. Gao, Z. Li, A. Jackering, G. Weber, J. Mican, Y. Chen, W. Dong, X. Han, C.G. Feiler, Y.F. Ao, C.P.S. Badenhorst, D. Bednar, G.J. Palm, M. Lammers, J. Damborsky, B. Strodel, W. Liu, U.T. Bornscheuer, R. Wei, Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase, ACS Catal, 12 (2022) 9790-9800.

[27] I.E. Meyer Cifuentes, P. Wu, Y. Zhao, W. Liu, M. Neumann-Schaal, L. Pfaff, J. Barys, Z. Li, J. Gao, X. Han, U.T. Bornscheuer, R. Wei, B. Ozturk, Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium, Front Bioeng Biotechnol, 10 (2022) 930140.

[28] S.R. Malwal, N. Shang, W. Liu, X. Li, L. Zhang, C.C. Chen, R.T. Guo, E. Oldfield, A Structural and Bioinformatics Investigation of a Fungal Squalene Synthase and Comparisons with Other Membrane Proteins, ACS Omega, 7 (2022) 22601-22612.

[29] Z. Li, Y. Zhao, P. Wu, H. Wang, Q. Li, J. Gao, H.M. Qin, H. Wei, U.T. Bornscheuer, X. Han, R. Wei, W. Liu, Structural insight and engineering of a plastic degrading hydrolase Ple629, Biochem Biophys Res Commun, 626 (2022) 100-106.

[30] Y. Hu, H. Li, J. Min, Y. Yu, W. Liu, J.W. Huang, L. Zhang, Y. Yang, L. Dai, C.C. Chen, R.T. Guo, Crystal structure and biochemical analysis of the specialized deoxynivalenol-detoxifying glyoxalase SPG from Gossypium hirsutum, Int J Biol Macromol, 200 (2022) 388-396.

[31] Q. Chen, B.-B. Li, L. Zhang, X.-R. Chen, X.-X. Zhu, F.-F. Chen, M. Shi, C.-C. Chen, Y. Yang, R.-T. Guo, W. Liu, J.-H. Xu, G.-W. Zheng, Engineered Imine Reductase for Larotrectinib Intermediate Manufacture, ACS Catal, 12 (2022) 14795-14803.

[32] F.Q. Chen, Y.P. Zhao, C.H. Zhang, W. Wang, J. Gao, Q. Li, H.M. Qin, Y.J. Dai, W.D. Liu, F.F. Liu, H. Su, X. Sheng, A Combined Computational-Experimental Study on the Substrate Binding and Reaction Mechanism of Salicylic Acid Decarboxylase, Catalysts, 12 (2022).

[33] C.-C. Chen, M. Dai, L. Zhang, J. Zhao, W. Zeng, M. Shi, J.-W. Huang, W. Liu, R.-T. Guo, A. Li, Molecular Basis for a Toluene Monooxygenase to Govern Substrate Selectivity, ACS Catalysis, 12 (2022) 2831-2839.

[34] W. Liu, C. Ma, W. Liu, Y. Zheng, C.C. Chen, A. Liang, X. Luo, Z. Li, W. Ma, Y. Song, R.T. Guo, T. Zhang, Functional and structural investigation of a novel beta-mannanase BaMan113A from Bacillus sp. N16-5, Int J Biol Macromol, 182 (2021) 899-909.

[35] N. Liu, L. Wu, J. Feng, X. Sheng, J. Li, X. Chen, J. Li, W. Liu, J. Zhou, Q. Wu, D. Zhu, Crystal Structures and Catalytic Mechanism of l-erythro-3,5-Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of beta-Amino Acids, Angew Chem Int Ed Engl, 60 (2021) 10203-10210.

[36] J. Li, G. Qu, N. Shang, P. Chen, Y. Men, W. Liu, Z. Mei, Y. Sun, Z. Sun, Near-perfect control of the regioselective glucosylation enabled by rational design of glycosyltransferases, Green Synthesis and Catalysis, 2 (2021) 45-53.

[37] L.G. Graf, E.A.P. Michels, Y. Yew, W. Liu, G.J. Palm, G. Weber, Structural analysis of PET-degrading enzymes PETase and MHETase from Ideonella sakaiensis, Methods Enzymol., 648 (2021) 337-356.

[38] X. Gao, M. Wu, W. Zhang, C. Li, R.T. Guo, Y. Dai, W. Liu, S. Mao, F. Lu, H.M. Qin, Structural Basis of Salicylic Acid Decarboxylase Reveals a Unique Substrate Recognition Mode and Access Channel, J Agric Food Chem, 69 (2021) 11616-11625.

[39] L. Dai, Z. Chang, J. Yang, W. Liu, Y. Yang, C.C. Chen, L. Zhang, J.W. Huang, Y. Sun, R.T. Guo, Structural investigation of a thermostable 1,2-beta-mannobiose phosphorylase from Thermoanaerobacter sp. X-514, Biochem Biophys Res Commun, 579 (2021) 54-61.

[40] Y. Cui, Y. Chen, X. Liu, S. Dong, Y.e. Tian, Y. Qiao, R. Mitra, J. Han, C. Li, X. Han, W. Liu, Q. Chen, W. Wei, X. Wang, W. Du, S. Tang, H. Xiang, H. Liu, Y. Liang, K.N. Houk, B. Wu, Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy, ACS Catalysis, 11 (2021) 1340-1350.

[41] C.C. Chen, S.R. Malwal, X. Han, W.D. Liu, L.X. Ma, C. Zhai, L.H. Dai, J.W. Huang, A. Shillo, J. Desai, X.Q. Ma, Y.H. Zhang, R.T. Guo, E. Oldfield, Terpene Cyclases and Prenyltransferases: Structures and Mechanisms of Action, ACS Catal, 11 (2021) 290-303.

[42] C.C. Chen, X. Han, X. Li, P.C. Jiang, D. Niu, L.X. Ma, W.D. Liu, S.Y. Li, Y.Y. Qu, H.B. Hu, J. Min, Y. Yang, L.L. Zhang, W. Zeng, J.W. Huang, L.H. Dai, R.T. Guo, General features to enhance enzymatic activity of poly(ethylene terephthalate) hydrolysis, Nature Catalysis, 4 (2021) 425-430.

[43] C. Chen, X. Han, W. Liu, L. Ma, K. Liu, R.T. Guo, [Structure-based engineering of PET hydrolase from Ideonella sakaiensis], Sheng Wu Gong Cheng Xue Bao, 37 (2021) 3268-3275.

[44] S. Zhou, T.P. Ko, J.W. Huang, W. Liu, Y. Zheng, S. Wu, Q. Wang, Z. Xie, Z. Liu, C.C. Chen, R.T. Guo, Structure of a gut microbial diltiazem-metabolizing enzyme suggests possible substrate binding mode, Biochem Biophys Res Commun, 527 (2020) 799-804.

[45] L. Zhang, Z. Xie, Z. Liu, S. Zhou, L. Ma, W. Liu, J.W. Huang, T.P. Ko, X. Li, Y. Hu, J. Min, X. Yu, R.T. Guo, C.C. Chen, Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase, Nat Commun, 11 (2020) 2676.

[46] X. Xiao, S.S. Elsayed, C. Wu, H.U. van der Heul, M. Metsa-Ketela, C. Du, A.E. Prota, C.C. Chen, W. Liu, R.T. Guo, J.P. Abrahams, G.P. van Wezel, Functional and Structural Insights into a Novel Promiscuous Ketoreductase of the Lugdunomycin Biosynthetic Pathway, ACS Chem. Biol., 15 (2020) 2529-2538.

[47] H. Sun, T.P. Ko, W. Liu, W. Liu, Y. Zheng, C.C. Chen, R.T. Guo, Structure of an antibiotic-synthesizing UDP-glucuronate 4-epimerase MoeE5 in complex with substrate, Biochem Biophys Res Commun, 521 (2020) 31-36.

[48] M. Song, X. Zhang, W. Liu, J. Feng, Y. Cui, P. Yao, M. Wang, R.T. Guo, Q. Wu, D. Zhu, 2,3-Dihydroxybenzoic Acid Decarboxylase from Fusarium oxysporum: Crystal Structures and Substrate Recognition Mechanism, ChemBioChem, 21 (2020) 2950-2956.

[49] H.M. Qin, D. Gao, M. Zhu, C. Li, Z. Zhu, H. Wang, W. Liu, M. Tanokura, F. Lu, Biochemical characterization and structural analysis of ulvan lyase from marine Alteromonas sp. reveals the basis for its salt tolerance, Int. J. Biol. Macromol., 147 (2020) 1309-1317.

[50] T.Z. Li, Z.J. Tang, H.L. Wei, Z.J. Tan, P. Liu, J.L. Li, Y.Y. Zheng, J.P. Lin, W.D. Liu, H.F. Jiang, H.F. Liu, L.L. Zhu, Y.H. Ma, Totally atom-economical synthesis of lactic acid from formaldehyde: combined bio-carboligation and chemo-rearrangement without the isolation of intermediates, Green Chem., 22 (2020) 6809-6814.

[51] J. Li, J.G. Yang, S.C. Mu, N. Shang, C. Liu, Y.M. Zhu, Y. Cai, P. Liu, J.P. Lin, W.D. Liu, Y.X. Sun, Y.H. Ma, Efficient O-Glycosylation of Triterpenes Enabled by Protein Engineering of Plant Glycosyltransferase UGT74AC1, ACS Catal, 10 (2020) 3629-3639.

[52] J.W. Huang, D. Niu, K. Liu, Q. Wang, L. Ma, C.C. Chen, L. Zhang, W. Liu, S. Zhou, J. Min, S. Wu, Y. Yang, R.T. Guo, Structure basis of non-structural protein pA151R from African Swine Fever Virus, Biochem Biophys Res Commun, 532 (2020) 108-113.

[53] C.C. Chen, J. Xue, W. Peng, B. Wang, L. Zhang, W. Liu, T.P. Ko, J.W. Huang, S. Zhou, J. Min, L. Ma, L. Dai, R.T. Guo, X. Yu, Structural insights into thebaine synthase 2 catalysis, Biochem Biophys Res Commun, 529 (2020) 156-161.

[54] C.C. Chen, L.H. Dai, L.X. Ma, R.T. Guo, Enzymatic degradation of plant biomass and synthetic polymers, Nat Rev Chem, 4 (2020) 114-126.

[55] C.-C. Chen, S.R. Malwal, X. Han, W. Liu, L. Ma, C. Zhai, L. Dai, J.-W. Huang, A. Shillo, J. Desai, X. Ma, Y. Zhang, R.-T. Guo, E. Oldfield, Terpene Cyclases and Prenyltransferases: Structures and Mechanisms of Action, ACS Catal, 11 (2020) 290-303.

[56] L. Zhang, T.P. Ko, S.R. Malwal, W. Liu, S. Zhou, X. Yu, E. Oldfield, R.T. Guo, C.C. Chen, Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism, Biochem Biophys Res Commun, 511 (2019) 800-805.

[57] K. Zhang, G. Qu, W. Liu, Z. Sun, [Structure-function relationships of industrial enzymes], Sheng Wu Gong Cheng Xue Bao, 35 (2019) 1806-1818.

[58] Z. Yang, L. Zhang, X. Yu, S. Wu, Y. Yang, Y. Hu, Q. Li, N. Shang, R.T. Guo, C.C. Chen, L. Dai, W. Liu, Crystal structure of TchmY from Actinoplanes teichomyceticus, Acta crystallographica. Section F, Structural biology communications, 75 (2019) 570-575.

[59] Y. Yang, L. Li, L. Yuan, X. Zhou, J. Duan, H. Xiao, N. Cai, S. Han, X. Ma, W. Liu, C.C. Chen, L. Wang, X. Li, J. Chen, N. Kang, J. Chen, Z. Shen, S.R. Malwal, W. Liu, Y. Shi, E. Oldfield, R.T. Guo, Y. Zhang, A Structural Change in Butyrophilin upon Phosphoantigen Binding Underlies Phosphoantigen-Mediated Vgamma9Vdelta2 T Cell Activation, Immunity, 50 (2019) 1043-1053 e1045.

[60] X. Tang, J. Xue, Y. Yang, T.P. Ko, C.Y. Chen, L. Dai, R.T. Guo, Y. Zhang, C.C. Chen, Structural insights into the calcium dependence of Stig cyclases, Rsc Adv, 9 (2019) 13182-13185.

[61] S.R. Malwal, L. Chen, H. Hicks, F. Qu, W. Liu, A. Shillo, W.X. Law, J. Zhang, N. Chandnani, X. Han, Y. Zheng, C.C. Chen, R.T. Guo, A. AbdelKhalek, M.N. Seleem, E. Oldfield, Discovery of Lipophilic Bisphosphonates That Target Bacterial Cell Wall and Quinone Biosynthesis, J Med Chem, 62 (2019) 2564-2581.

[62] J. Ma, T.P. Ko, X. Yu, L. Zhang, L. Ma, C. Zhai, R.T. Guo, W. Liu, H. Li, C.C. Chen, Structural insights to heterodimeric cis-prenyltransferases through yeast dehydrodolichyl diphosphate synthase subunit Nus1, Biochem Biophys Res Commun, 515 (2019) 621-626.

[63] C.J. Kuo, J. Gao, J.W. Huang, T.P. Ko, C. Zhai, L. Ma, W. Liu, L. Dai, Y.F. Chang, T.H. Chen, Y. Hu, X. Yu, R.T. Guo, C.C. Chen, Functional and structural investigations of fibronectin-binding protein Apa from Mycobacterium tuberculosis, Biochim. Biophys. Acta, Gen. Subj., 1863 (2019) 1351-1359.

[64] T.P. Ko, X. Xiao, R.T. Guo, J.W. Huang, W. Liu, C.C. Chen, Substrate-analogue complex structure of Mycobacterium tuberculosis decaprenyl diphosphate synthase, Acta crystallographica. Section F, Structural biology communications, 75 (2019) 212-216.

[65] S. Han, X. Li, Y. Xia, Z. Yu, N. Cai, S.R. Malwal, X. Han, E. Oldfield, Y. Zhang, Farnesyl Pyrophosphate Synthase as a Target for Drug Development: Discovery of Natural-Product-Derived Inhibitors and Their Activity in Pancreatic Cancer Cells, J Med Chem, 62 (2019) 10867-10896.

[66] Y. Feng, X. Yu, J.W. Huang, W. Liu, Q. Li, Y. Hu, Y. Yang, Y. Chen, J. Jin, H. Li, C.C. Chen, R.T. Guo, Crystal structure and proposed mechanism of an enantioselective hydroalkoxylation enzyme from Penicillium herquei, Biochem Biophys Res Commun, 516 (2019) 801-805.

[67] X. Chen, H.L. Zhang, M.A. Maria-Solano, W.D. Liu, J. Li, J.H. Feng, X.T. Liu, S. Osuna, R.T. Guo, Q.Q. Wu, D.M. Zhu, Y.H. Ma, Efficient reductive desymmetrization of bulky 1,3-cyclodiketones enabled by structure-guided directed evolution of a carbonyl reductase, Nature Catalysis, 2 (2019) 931-941.

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