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. Author manuscript; available in PMC: 2006 Jan 20.
Published in final edited form as: J Biol Chem. 2005 Oct 14;280(49):40668–40675. doi: 10.1074/jbc.M509748200

Fig. 3.

Fig. 3

NMR spectrum of 1.6 mM GLX2-5. NMR spectra were collected on a Bruker Avance 500 spectrometer operating at 500.13 MHz, 298 K, and a magnetic field of 11.7 T, recycle delay (AQ), 41 ms; sweep width, 400 ppm. Protein chemical shifts were calibrated by assigning the H2O signal the value of 4.70 ppm. A modified presaturation pulse sequence (zgpr) was used to suppress the proton signals originating from water molecules.