Kandegedara, A., Rorabacher, D.B. (1999) Noncomplexing Tertiary Amines as “Better” Buffers Covering the Range of pH 3− 11. Temperature Dependence of Their Acid Dissociation Constants. Anal. Chem., 71 (15), 3140–3144.
-The paper examines a number of buffers developed by Good (often called “Good’s” or “Good” buffers) have been shown to cause metal ion interference as a result of complexation. This can be critical in protein crystallization especially if metals are needed for proper protein folding. A series of tertiary amines, devoid of hydroxy groups or other weak donors on the r, â, or ç carbons, have been developed as “Better” pH buffers which, as a result of steric hindrance, are incapable of forming even weak complexes with metal ions. MOPS, MES and PIPES are the only three of the twenty Good Buffers that were examined that do not show weak coordination. Unfortunately, PIPES can be limited due to solubility in biologically relevant conditions.

Goldber, DA. (1980) Isolation and partial characterization of the Drosophila alcohol dehydrogenase gene. Proc. Natl. Acad. Sci. USA. Vol. 77, 5794-5798.

Oldfield, TJ. Ceska, TA. Brady, RL. (1991) A flexible approach to automated protein crystallization. Journal of Applied Crystallography. Vol. 24. 255-260.
-MOPS is used as an example buffer in this paper discussing a set up for automated protein crystallization.