Faculty Publications

Crystallization and Structure Determination of Bovine Profilin at 2·0 Å Resolution

Document Type

Article

Journal/Book/Conference Title

Journal of Molecular Biology

Volume

240

Issue

5

First Page

459

Last Page

475

Abstract

Profilin regulates the behavior of the eukaryotic microfilament system through its interaction with non-filamentous actin. It also binds several ligands, including poly(l-proline) and the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Bovine profilin crystals (space group C2; a = 69·15 Å, b = 34·59 Å, c = 52·49 Å; α = γ = 90°, β = 92·56°) were grown from a mixture of poly(ethylene glycol) 400 and ammonium sulfate. X-ray diffraction data were collected on an imaging plate scanner at the DORIS storage ring (DESY, Hamburg), and were phased by molecular replacement, using a search model derived from the 2·55 Å structure of profilin complexed to β-actin. The refined model of bovine profilin has a crystallographic R -factor of 16·5% in the resolution range 6·0 to 2·0 Å and includes 128 water molecules, several of which form hydrogen bonds to stabilize unconventional turns.

Department

Department of Chemistry and Biochemistry

Original Publication Date

7-28-1994

DOI of published version

10.1006/jmbi.1994.1461

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