NDLI: Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.

Please wait, while we are loading the content...

Spatial and temporal distribution of Î³H2AX fluorescence in human cell cultures following synchrotron-generated X-ray microbeams: lack of correlation between persistent Î³H2AX foci and apoptosis.

A tunable wedge-shaped absorber for hard X-ray synchrotron applications.

Exploiting coherence for real-time studies by single-bunch imaging.

The multi-purpose hard X-ray beamline BL10 at the DELTA storage ring.

Hard X-ray nanotomography beamline 7C XNI at PLS-II.

Comments on structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 Å resolution by P. Ramesh et al. (2013). J. Synchrotron Rad.20, 843-847.

Response to comments on structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 Å resolution by P. Ramesh et al. (2013). J. Synchrotron Rad. 20, 843-847.

Year: 2014 Volume: 21 Issue: Part 3

Year: 2014 Volume: 21 Issue: Part 2

Year: 2014 Volume: 21 Issue: Part 1

Year: 2013 Volume: 20

Year: 2012 Volume: 19

Year: 2011 Volume: 18

Year: 2010 Volume: 17

Year: 2009 Volume: 16

Year: 2008 Volume: 15

Year: 2007 Volume: 14

Year: 2006 Volume: 13

Year: 2001 Volume: 8

Year: 1999 Volume: 6

Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gupta, Sayan Celestre, Richard Petzold, Christopher J. Chance, Mark R. Ralston, Corie
Description	Country affiliation: United States Author Affiliation: Gupta S ( Berkeley Center for Structural Biology, Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.); Celestre R ( Experimental Systems, Advanced Light Source Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.); Petzold CJ ( Joint BioEnergy Institute, Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.); Chance MR ( Center for Synchrotron Biosciences, Center for Proteomics and Bioinformatics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.); Ralston C ( Berkeley Center for Structural Biology, Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.)
Abstract	X-ray footprinting (XF) is an important structural biology tool used to determine macromolecular conformations and dynamics of both nucleic acids and proteins in solution on a wide range of timescales. With the impending shut-down of the National Synchrotron Light Source, it is ever more important that this tool continues to be developed at other synchrotron facilities to accommodate XF users. Toward this end, a collaborative XF program has been initiated at the Advanced Light Source using the white-light bending-magnet beamlines 5.3.1 and 3.2.1. Accessibility of the microsecond time regime for protein footprinting is demonstrated at beamline 5.3.1 using the high flux density provided by a focusing mirror in combination with a micro-capillary flow cell. It is further reported that, by saturating samples with nitrous oxide, the radiolytic labeling efficiency is increased and the imprints of bound versus bulk water can be distinguished. These results both demonstrate the suitability of the Advanced Light Source as a second home for the XF experiment, and pave the way for obtaining high-quality structural data on complex protein samples and dynamics information on the microsecond timescale.
File Format	HTM / HTML
ISSN	09090495
e-ISSN	16005775
DOI	10.1107/S1600577514007000
Journal	Journal of Synchrotron Radiation
Issue Number	Pt 4
Volume Number	21
Language	English
Publisher	IUCr
Publisher Date	2014-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Radiology Crystallography, X-ray Instrumentation Protein Footprinting Proteins Chemistry Ultrastructure Synchrotrons Binding Sites Equipment Design Equipment Failure Analysis Protein Binding Protein Conformation Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Nuclear and High Energy Physics Instrumentation Radiation

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Structural Biology Center 19ID undulator beamline: facility specifications and protein crystallographic results.

Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source

Recent Advances in X-Ray Hydroxyl Radical Footprinting at the Advanced Light Source Synchrotron.

Crystal structure of rat liver dihydropteridine reductase.

Mini-beam collimator enables microcrystallography experiments on standard beamlines.

Goniometer-based femtosecond crystallography with X-ray free electron lasers.

Lipidic phase membrane protein serial femtosecond crystallography.

Observation of the light-triggered binding of pyrone to chymotrypsin by Laue x-ray crystallography.

Unique MAP Kinase binding sites.

Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.

Similar Documents

The Structural Biology Center 19ID undulator beamline: facility specifications and protein crystallographic results.

Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source

Recent Advances in X-Ray Hydroxyl Radical Footprinting at the Advanced Light Source Synchrotron.

Crystal structure of rat liver dihydropteridine reductase.

Mini-beam collimator enables microcrystallography experiments on standard beamlines.

Goniometer-based femtosecond crystallography with X-ray free electron lasers.

Lipidic phase membrane protein serial femtosecond crystallography.

Observation of the light-triggered binding of pyrone to chymotrypsin by Laue x-ray crystallography.

Unique MAP Kinase binding sites.

Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.