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2006
MaesD, CrabeelM, Van deWeerdt C, MartialJ, PeetersE, CharlierD, DecanniereK, VanheeC, WynsL, ZegersI.  2006.  Crystallization of ornithine acetyltransferase from yeast by counter-diffusion and preliminary X-ray study. 62(Pt 12):1294-1297. Abstract
2005
WillaertR, ZegersI, WynsL, SleutelM.  2005.  Protein crystallization in hydrogel beads. 61(Pt 9):1280-1288. Abstract
2003
LahN, LahJ, ZegersI, WynsL, MessensJ.  2003.  Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus. J. Biol. Chem.. 278(27):24673-24679. Abstract
MessensJ, MartinsJC, ZegersI, VanBelle K, BrosensE, WynsL.  2003.  Purification of an oxidation-sensitive enzyme, pI258 arsenate reductase from Staphylococcus aureus. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.. 790(1-2):217-227. Abstract
VerseesW, VanHolsbeke E, DeVos S, DecanniereK, ZegersI, SteyaertJ.  2003.  Cloning, preliminary characterization and crystallization of nucleoside hydrolases from Caenorhabditis elegans and Campylobacter jejuni. Acta Crystallographica D. 59(Pt 6):1087-1089. Abstract
2002
MessensJ, MartinsJC, VanBelle K, BrosensE, DesmyterA, DeGieter M, WieruszeskiJM, WillemR, WynsL, ZegersI.  2002.  All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade. Proc. Natl. Acad. Sci. USA. 99(13):8506-8511. Abstract
2001
ZegersI, MartinsJC, WillemR, WynsL, MessensJ.  2001.  Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty. Nat. Struct. Biol.. 8(10):843-847. Abstract
1999
ZegersI, DeswarteJ, WynsL.  1999.  Trimeric domain-swapped barnase. 96(3):818-822. Abstract
1998
ZegersI, LorisR, DehollanderG, FattahHaikal A, PoortmansF, SteyaertJ, WynsL.  1998.  Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. 5(4):280-283. Abstract
ZegersI, LorisR, DehollanderG, FattahHaikal A, PoortmansF, SteyaertJ, WynsL.  1998.  Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. 5(4):280-283. Abstract
1996
DoumenJ, GonciarzM, ZegersI, LorisR, WynsL, SteyaertJ.  1996.  A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1. 5(8):1523-1530. Abstract
DoumenJ, GonciarzM, ZegersI, LorisR, WynsL, SteyaertJ.  1996.  A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1. 5(8):1523-1530. Abstract
1994
ZegersI, MaesD, Dao-ThiMH, PoortmansF, PalmerR, WynsL.  1994.  The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules. 3(12):2322-2339. Abstract
PletinckxJ, SteyaertJ, ZegersI, ChoeHW, HeinemannU, WynsL.  1994.  Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution. Biochemistry. 33(7):1654-1662. Abstract
PletinckxJ, SteyaertJ, ZegersI, ChoeHW, HeinemannU, WynsL.  1994.  Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution. 33(7):1654-1662. Abstract
ZegersI, HaikalAF, PalmerR, WynsL.  1994.  Crystal structure of RNase T1 with 3'-guanylic acid and guanosine. 269(1):127-133. Abstract
1993
LisgartenJN, GuptaV, MaesD, WynsL, ZegersI, PalmerRA, DealwisCG, AguilarCF, HemmingsAM.  1993.  Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures. 49(Pt 6):541-547. Abstract
SevcikJ, ZegersI, WynsL, DauterZ, WilsonKS.  1993.  Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate. 216(1):301-305. Abstract
1992
ZegersI, VerhelstP, ChoeHW, SteyaertJ, HeinemannU, SaengerW, WynsL.  1992.  Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant. Biochemistry. 31(46):11317-11325. Abstract
ZegersI, VerhelstP, ChoeHW, SteyaertJ, HeinemannU, SaengerW, WynsL.  1992.  Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant. 31(46):11317-11325. Abstract

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