Crystallization and preliminary X-ray crystallographic analysis of SP1, a novel chaperone-like protein

Wangxia Wang, Or Dgany, Orly Dym, Arie Altman, Oded Shoseyov, Orna Almog*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

SP1 (108 amino acids) is a boiling-stable stress-responsive protein. It has no significant sequence homology to other stress-related proteins or to small heat-shock proteins (sHsps). SP1 activity is ATP-independent, similar to other small heat-shock proteins. Based on these features, it is expected that the structure-function relationship of SP1 will be unique. In this work, the crystallization and preliminary crystallographic data of native SP1 and its selenomethionine derivative are described. Recombinant SP1 and its selenomethionine derivative were expressed in Escherichia coli and used for crystallization experiments. SP1 crystals were grown from 0.1 M HEPES pH 7.5, 20% PEG 3K, 0.2 M NaCl. One to four single crystals appeared in each droplet within a few days and grew to dimensions of about 0.5 × 0.5 × 0.8 mm after about two weeks. Diffraction studies of these crystals at low temperature indicated that they belong to space group I422, with unit-cell parameters a = 89, b = 89, c = 187 Å. Efforts to crystallize the selenomethionine derivative of SP1 are in progress.

Original languageAmerican English
Pages (from-to)512-514
Number of pages3
JournalActa Crystallographica Section D: Structural Biology
Volume59
Issue number3
DOIs
StatePublished - 1 Mar 2003

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X-ray crystallographic analysis of SP1, a novel chaperone-like protein'. Together they form a unique fingerprint.

Cite this