Crystallization of a pentapeptide-repeat protein by reductive cyclic pentylation of free amines with glutaraldehyde. Export

@article{Vetting2009, abstract = {The pentapeptide-repeat protein EfsQnr from Enterococcus faecalis protects DNA gyrase from inhibition by fluoroquinolones. EfsQnr was cloned and purified to homogeneity, but failed to produce diffraction-quality crystals in initial crystallization screens. Treatment of EfsQnr with glutaraldehyde and the strong reducing agent borane-dimethylamine resulted in a derivatized protein which produced crystals that diffracted to 1.6 A resolution; their structure was subsequently determined by single-wavelength anomalous dispersion. Analysis of the derivatized protein using Fourier transform ion cyclotron resonance mass spectrometry indicated a mass increase of 68 Da per free amino group. Electron-density maps about a limited number of structurally ordered lysines indicated that the modification was a cyclic pentylation of free amines, producing piperidine groups.}, author = {Vetting, Matthew W. and Hegde, Subray S. and Blanchard, John S.}, citeulike-article-id = {4362837}, citeulike-linkout-0 = {http://dx.doi.org/10.1107/S0907444909008324}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19390151}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19390151}, doi = {10.1107/S0907444909008324}, issn = {1399-0047}, journal = {Acta crystallographica. Section D, Biological crystallography}, keywords = {beta\_helix, beta\_solenoid, pentapeptide\_repeat}, month = {May}, number = {Pt 5}, pages = {462--469}, posted-at = {2009-09-21 12:38:59}, priority = {2}, publisher = {International Union of Crystallography}, title = {Crystallization of a pentapeptide-repeat protein by reductive cyclic pentylation of free amines with glutaraldehyde.}, url = {http://dx.doi.org/10.1107/S0907444909008324}, volume = {65}, year = {2009} }

TY - JOUR ID - Vetting2009 L3 - citeulike-article-id:4362837 N2 - The pentapeptide-repeat protein EfsQnr from Enterococcus faecalis protects DNA gyrase from inhibition by fluoroquinolones. EfsQnr was cloned and purified to homogeneity, but failed to produce diffraction-quality crystals in initial crystallization screens. Treatment of EfsQnr with glutaraldehyde and the strong reducing agent borane-dimethylamine resulted in a derivatized protein which produced crystals that diffracted to 1.6 A resolution; their structure was subsequently determined by single-wavelength anomalous dispersion. Analysis of the derivatized protein using Fourier transform ion cyclotron resonance mass spectrometry indicated a mass increase of 68 Da per free amino group. Electron-density maps about a limited number of structurally ordered lysines indicated that the modification was a cyclic pentylation of free amines, producing piperidine groups. IS - Pt 5 JF - Acta crystallographica. Section D, Biological crystallography SN - 1399-0047 EP - 469 TI - Crystallization of a pentapeptide-repeat protein by reductive cyclic pentylation of free amines with glutaraldehyde. PB - International Union of Crystallography VL - 65 SP - 462 KW - beta_helix KW - beta_solenoid KW - pentapeptide_repeat AU - Vetting, Matthew AU - Hegde, Subray AU - Blanchard, John PY - 2009/05// UR - http://dx.doi.org/10.1107/S0907444909008324 ER -