Solution NMR has become an indispensable technique in studying the physical properties and functions of biomacromolecules at near physiological conditions. However, biomolecular systems are often extraordinarily large, dynamic, and possess low solubility, which complicates the acquisition and analysis of NMR spectra. Together this results in severe signal overlapping and low signal to noise, which demands longer total experimental time. NMR spectroscopists must consider how to improve spectral resolution and sensitivity to extract the maximum structural information from imperfect data within reasonable measurement times. Recent advances in multi-dimensional NMR acquisition and computation methods overcome these problems and enable the investigation of larger and more complicated biomolecular systems. This chapter first reviews conventional and then state-of-the-art methodologies for NMR data collection, signal processing, and protein structure data analysis. In the first section, we survey the basics of multi-dimensional NMR and present rapid measurement techniques such as non-uniform sampling and spectrum reconstruction algorithms. In the second half, we illustrate the conventions of protein structure determination using chemical shift and NOE data to obtain interatomic distances, dihedral angles, and dynamics information. We also briefly introduce the currently popular hybridisation of NMR with solution angle scattering for 3D structure analysis.