Preliminary crystallographic analysis of the cysteine desulfurase IscS from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1224-5. doi: 10.1107/s0907444902007370. Epub 2002 Jun 20.

Abstract

IscS is a widely distributed cysteine desulfurase that catalyzes the pyridoxal phosphate dependent beta-elimination of sulfur from L-cysteine and plays a central role in the delivery of sulfur to a variety of metabolic pathways. Crystals of Escherichia coli IscS have been obtained by the hanging-drop vapor-diffusion method using polyethylene glycol (PEG) as a precipitant. Initial seed crystals were obtained using PEG 6000 and sodium acetate, and diffraction-quality crystals were grown using a mixture of PEG 2000 and PEG 10 000 in the presence of sodium citrate. A complete native X-ray diffraction data set was collected from a single crystal at 103 K to a resolution of 2.1 A. The crystals belong to space group P2(1)2(1)2(1) and have unit-cell parameters a = 73.7086, b = 101.9741, c = 108.617 A (alpha = beta = gamma = 90 degrees ). Analysis of the Matthews equation and self-rotation function suggest two molecules per asymmetric unit, consistent with the presence of a single dimeric molecule.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carbon-Sulfur Lyases / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray / methods*
  • Dimerization
  • Escherichia coli / enzymology
  • Polyethylene Glycols / chemistry

Substances

  • Polyethylene Glycols
  • Carbon-Sulfur Lyases
  • cysteine desulfurase