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Structure of D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor in a tetragonal crystal form

Structure of D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor in a tetragonal crystal form
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摘要 D-glyceraldehyde-3-phosphate dehydrogenase (holo-GAPDH) from Palinurus versicolor was crystallized in a novel crystal form by the method of sitting-drop vapor diffusion. The crystals have space group P4212, cell parameters a=15.49 nm, c=8.03 nm and two subunits per asymmetric unit. The crystal structure at 0.34 nm was determined by the molecular replacement method. The final model has crystallographic Rfree and R factors of 0.274 and 0.262, and r.m.s. deviations of 0.002 nm for bond lengths and 2.33?for bond angles. The two subunits in asymmetric unit are similar to each other not only in the three-dimensional structure, but also in average temperature factors. This result demonstrates that the obvious difference in average temperature factors for the different subunits in C2 crystal form reported previously may be attributed to the different crystallographic environments of the subunits. This further supports that holo-GAPDH has a good 222 molecular symmetry. D-glyceraldehyde-3-phosphate dehydrogenase (holo-GAPDH) from Palinurus versicolor was crystallized in a novel crystal form by the method of sitting-drop vapor diffusion. The crystals have space group P4212, cell parameters a=15.49 nm, c=8.03 nm and two subunits per asymmetric unit. The crystal structure at 0.34 nm was determined by the molecular replacement method. The final model has crystallographic Rfree and R factors of 0.274 and 0.262, and r.m.s. deviations of 0.002 nm for bond lengths and 2.33?for bond angles. The two subunits in asymmetric unit are similar to each other not only in the three-dimensional structure, but also in average temperature factors. This result demonstrates that the obvious difference in average temperature factors for the different subunits in C2 crystal form reported previously may be attributed to the different crystallographic environments of the subunits. This further supports that holo-GAPDH has a good 222 molecular symmetry.
出处 《Science China(Life Sciences)》 SCIE CAS 2000年第1期96-104,共9页 中国科学(生命科学英文版)
关键词 D-glyceraldehyde-3-phosphate dehydrogenase ALLOSTERIC enzyme and crystal structure. D-glyceraldehyde-3-phosphate dehydrogenase, allosteric enzyme and crystal structure.
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参考文献2

  • 1Matthews,B.W.Solvent content of protein crystals, J[].Molecular Biology.1968
  • 2Levitzki,A.Half-of-the-sites and all-of-the-sites reactivity in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase, J[].Molecular Biology.1974

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