The role of entropy and polarity in intermolecular contacts in protein crystals.

ABSTRACT: The integrity and X-ray diffraction quality of protein crystals depend on the three-dimensional order of relatively weak but reproducible intermolecular contacts. Despite their importance, relatively little attention has been paid to the chemical and physical nature of these contacts, which are often regarded as stochastic and thus not different from randomly selected protein surface patches. Here, logistic regression was used to analyze crystal contacts in a database of 821 unambiguously monomeric proteins with structures determined to 2.5 A resolution or better. It is shown that the propensity of a surface residue for incorporation into a crystal contact is not a linear function of its solvent-accessible surface area and that amino acids with low exposed surfaces, which are typically sma

SUBMITTER: Cieslik M 

PROVIDER: S-EPMC2672819 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature