Isolation and crystallization of bacterial porin.

TLDR: Porin has proven to be rather useful for the optimization of conditions to crystallize membrane proteins as it is very stable over a wide range of conditions Crystallization experiments (at 20°) are successful also using several other detergents with a moderate to high carboxymethyl cellulose (CMC) initial problems with reproducibility of porin crystallization revealed that a high degree of purity of this protein is required, and that the removal of tightly bound lipoprotein and glycolipid is critical for success as mentioned in this paper.

Abstract: Publisher Summary This chapter describes isolation and crystallization of bacterial porin The unusual aspects of porin crystallization are consistent with the micellar interactions involved in crystal formation The resulting porin crystals are relatively sensitive to the environment Care must be taken in handling and mounting crystals for X-ray analysis to avoid significant or abrupt changes in the solvent or detergent environment and uncontrolled variations of temperature Porin has proven to be rather useful for the optimization of conditions to crystallize membrane proteins as it is very stable over a wide range of conditions Crystallization experiments (at 20°) are successful also using several other detergents with a moderate to high carboxymethyl cellulose (CMC) Initial problems with reproducibility of porin crystallization revealed that a high degree of purity of this protein is required, and that the removal of tightly bound lipoprotein and glycolipid is critical for success Although current experience is limited, it seems fair to conclude that with a better understanding of protein–amphiphile interactions, of micellar physical chemistry, and with improvement in crystallization techniques, the outlook for understanding membrane protein structure appears bright