Structural Biology at NIH - X-ray crystallography

Group picture from left to right: Christian, Lisa, Gabi (postdoc of M. Gellert), Jae Young, Shikha (joint postdoc of M. Gellert), Marcin, Santiago, Feng and Wei

Senior Investigator: Dr. Wei Yang

Affiliation: Section on Molecular Structure, LMB, NIDDK.

Research: Molecular assemblies and mechanisms of DNA recombination and repair, particularly the V(D)J gene rearrangement in immune system and methyl-directed mismatch MutSLH repair system.

Personnel : Christian Biertuempfel , Shikha Gupta , Chris Larkin , Jae Young Lee , Marcin Nowotny , Santiago Ramon-Maiques , Feng Wang , and Lan Tian

Summer Interns : Judy Chang, Emily Deye, Jessamine Winer, Isabelle Winer and Mark Gregory

Former lab members : Changill Ban , Alba Guarne , James Hu , Fred Jerva , Murray Junop , Hong Ling , Kelly Rausch , Qinghai Zhao and Lisa Eiben

Equipment and Resources: the group has independent wetlab, cold room, and office space. The X-ray and some computer equipment is shared with the other crystallography groups in the building.

  • Positions available

  • Postdoctoral positions We are currently working on DNA mismatch repair, translesion DNA synthesis, V(D)J recombination, and various metal ion-dependent enzymes. The techniques routinely required are cloning, protein expression (in bacterial, insect or mammalian cells) and purification, kinetic assays of protein and nucleic acid binding and catalysis, X-ray crystallography, and mutagenesis and functional studies. Candidates, who have prior training in protein and nucleic acid chemistry, kinetics of catalysis, or molecular and cellular biology and are keen to crystallography are welcome to apply. Candidates are required to have less than 1 year of postdoctoral experience. Please send an application letter, CV and 3 references to Wei Yang by email or to LMB, NIDDK, NIH, Bldg. 5, Rm B1-03, 9000 Rockville Pike, Bethesda, MD 20892.

    Some Recent Publications: (Electronic Reprint Ordering System)

    Nowotny, M. and Yang, W. (2006). "Stepwise analyses of metal ions in RNase H catalysis: from substrate destabilization to product release". EMBO J. , epub ahead of print, April 6, 2006.

    Yang, W., Lee, J. Y. and Marcin, N. (2006). "Making and breaking nucleic acids: two- Mg2+-ion catalysis and substrate specificity". Mol Cell, 22, 5-13.

    Yang, W.. (2006). "Poor base stacking at DNA lesions may initiate recognition by many repair proteins". DNA Repair , ePub ahead of print, March 27, 2006.

    Lee, J. Y., Chang, J., Joseph, N. Ghirlando, R., Desirazu, N. R., and Yang, W. (2005). "MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage". Mol. Cell, 20, 155-166.

    Vaisman A., Ling, H., Woodgate, R., and Yang, W. (2005). "Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis". EMBO J. 24, 2957- 2967.

    Nowotny, M., Gaidamakov, S. A., Crouch, R. J., and Yang, W. (2005). "Crystal structures of RNase H bound to an RNA: substrate specificity and metal-dependent catalysis". Cell , 121, 1005-16.

    Guarne, A., Brendler T., Zhao, Q., Ghirlando, R., Austin, S., and Yang, W. (2005). "Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization". EMBO J. , 24, 1502-1511.

    Yang, W. (2005) "Portraits of a Y-family DNA polymerase", FEBS Lett., 579, 868-72.

    Guarne, A., Ramon-Maiques, S., Wolff, E. M., Ghirlando, R., Hu, X., Miller, J. H., and Yang, W. (2004). "Structure of the MutL C-terminal domain: a model of intact Mutl and its roles in mismatch repair". EMBO J. , 23, 4134-45.

    Ling, H, Boudsocq, F., Woodgate, R. and Yang, W. (2004). "Snapshots of replication through an abasic lesion: structural basis for base substitution and frameshift", Mol Cell , 13, 751-762.

    Ling, H, Sayer, J.M., Plosky, B.S., Yagi, H., Boudsocq, F., Woodgate, R., Jerina, D. M. and Yang, W. (2004). "Crystal structure of a benzo[a]pyrene diol epoxide adduct in a ternary complex with a DNA polymerase". PNAS , 101, 2265-2269.

    Ling, H, Boudsocq, F., Plosky, B., Woodgate, R. and W. Yang (2003). "Replication of a cis-syn thymine dimer at atomic resolution". Nature , 424, 1083-1087.

    Hu, X., Machius, M., and W. Yang (2003). "Monovalent cation dependence and pre- ference of GHKL ATPases and kinases". FEBS Lett. 544, 268-273.

    Junop, M. S., W. Yang, Funchain, P., Clendenin, W. and Jeffrey H. Miller (2003). "In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination" DNA Repair , 2, 387-405.

    W. Yang (2003), "DNA damage repair polymerase Y". Curr. Opin. Struct. Biol. 13, 23-30.

    Guarne, A., Zhao, Q.-H. Ghirlando, R.. and W. Yang (2002). "SeqA complexed with hemimethylated DNA: negative modulation of E. coli >replication initiation" Nat. Struct. Biol. , 9, 839-843.

    Wang, J.-J., Ling H., W. Yang and Craigie, R. (2001). "Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein". EMBO J., 20, 7333-7343.

    Guarné, A., Junop, M. S. & W. Yang (2001). EMBO J. 20:5521-5531. Structure and function of the N-terminal 40kDa fragment of human PMS2: a monomeric GHL ATPase.

    Ling H., Boudsocq F., Woodgate R. & W. Yang (2001). Cell 107:91-102. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypassreplication.

    Junop M. S., Obmolova G., Rausch K., Hsieh P. & W. Yang (2001). Mol. Cell 7:1-12. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair.

    Yang W. , Junop, M. S., Ban, C., Obmolova, G., Hsieh, P. (2000). Cold Spring Harbor Symposium on Biological responses to DNA damage, 65 :225-232. DNA mismatch repair: From structure to mechanism.

    Junop M. S., Modesti M., Guarne A., Ghirlando R., Gellert M. & W. Yang (2000). EMBO J. 19:5962-5970. Crystal structure of the Xrcc4 DNA repair protein and implications for end joining.

    Obmolova G., Ban C., Hsieh P. & W. Yang (2000). Nature 407:703-710. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA.

    W. Yang (2000). Mutat. Res. 460:245-256. Structure and function of mismatch repair proteins.

    Ban C., Junop M. & W. Yang (1999). Cell 97:85-97. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair.

    Ban C. & W. Yang (1998). Cell 95:541-552. Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis.

    Ban C. & W. Yang (1998). EMBO J. 17:1526-1534. Structural basis for MutH activation in E. coli mismatch repair and relationship of MutH to restriction endonucleases.

    Contact: Dr. Wei Yang, Bldg. 5, Room B103. NIDDK, NIH, Bethesda, MD 20892.

    E-mail: Wei.Yang@nih.gov

    This page is maintained by Wei Yang.
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