Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method.

ABSTRACT: Crystals of human triosephosphate isomerase with two crystal morphologies were obtained using the normal vapour-diffusion technique with identical crystallization conditions. One had a disordered plate shape and the crystals were hollow (crystal form 1). As a result, this form was very fragile, diffracted to 2.8 A resolution and had similar crystallographic parameters to those of the structure 1hti in the Protein Data Bank. The other had a fine needle shape (crystal form 2) and was formed more abundantly than crystal form 1, but was unsuitable for structure analysis. Since the normal vapour-diffusion method could not control the crystal morphology, gel-tube methods, both on earth and under microgravity, were applied for crystallization in order to control and improve the crystal quality. W

SUBMITTER: Kinoshita T 

PROVIDER: S-EPMC1952429 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature