EC Number   |
|---|
    2.1.1.45 | - |
| 2.1.1.45 | apo-enzyme crystallized in the active form with sulfate ions |
| 2.1.1.45 | co-crystallization of the purified enzyme with inhibitor 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid and FdUMP in the TS site and NADPH and methotrexate in the DHFR site, X-ray diffraction structure determination and analysis at 3.45 A resolution, PDB ID 4Q0D |
| 2.1.1.45 | crystallized in the I2(1)3 space group |
| 2.1.1.45 | crystals belong to space group P2(1)2(1)2(1), a = 54.05 A, b = 66.16 A and c = 178.76 A |
| 2.1.1.45 | crystals grown by the hanging drop vapor diffusion method |
| 2.1.1.45 | crystals grown by vapor diffusion method in hanging drop setup |
| 2.1.1.45 | crystals of TS apoprotein grown using hanging drop method of vapor diffusion, cubic Laue group m3 with a = 133 A |
| 2.1.1.45 | determination of chemical shifts of the apoenzyme (lig0), the saturated holoenzyme (lig2), and the typically elusive singly bound (lig1) states. The two active sites in TS communicate with one another by using the intervening beta-sheet that also forms the dimer interface. The active sites have minimal communication in the lig0 state, but rather a network of correlated motions involving the two active sites is triggered by the first diligand binding event and amplified upon binding the second. Contacts between the diligand and a right-handed beta-bulge feature of this sheet are likely the triggering events |
| 2.1.1.45 | grown in low-salt conditions, 100 mM Tris, pH 9.0, 20 mM beta-mercaptoethanol, 3 mM KH2PO4, and 10-20% PEG 4K, by hanging drop diffusion at 4 °C |
