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Bacterial adhesin / Bacteriology / Microbiology / Cell adhesion / Complement control protein / Ribosome / Protein structure / Bordetella / Chaperone / Biology / Proteins / Protein biosynthesis


THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 281, NO. 31, pp[removed]–22377, August 4, 2006 © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. Crystal Structure and Mutational
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Document Date: 2006-08-18 02:11:22


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City

Ann Arbor / Uppsala / La Jolla / Foster City / San Diego / /

Company

Protein Data Bank / AfaE-III / NUMBER 31 AB / DraE / DaaE Adhesin Analysis / BIAcore AB / Stanford Synchrotron Radiation Laboratory / CCP / Molecular Biology Inc. / AfaE-V / Amersham Biosciences / compared using the DaaE / /

Country

Sweden / United Kingdom / /

Currency

pence / /

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Facility

AfaE-III-DAF complex / C terminus / University of Washington Health Sciences Libraries / Stanford University / Institute of Virology / University of Glasgow / Stanford Synchrotron Radiation Laboratory / Oxford University / University of Washington / DraE-DAF complex / Rutgers University / National Institute of General Medical Sciences / N terminus / terminal G-strand / University of Michigan / /

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IndustryTerm

comparative modeling protocol / structure prediction server / metal affinity chromatography / free energy / insertion site / balanced saline solution / sensor chips / mg/ml protein solution / research-grade sensor chip / double-subtraction protocol / conserved site / overall free energy / polypeptide chain / /

MedicalCondition

strain / ALS / diarrhea / urinary tract infections / infections / Bordetella pertussis / cystitis / protracted diarrhea / pyelonephritis / /

MedicalTreatment

antibiotics / /

MusicGroup

O / /

Organization

¶Biomolecular Structure Center / Institute of Virology / University of Washington Health Sciences Libraries / Rutgers University / University of Michigan / University of Glasgow / United States Department of Energy / office of Biological and Environmental Research / National Institute of General Medical Sciences / office of Science / Department of Biological Structure / Department of Microbiology / School of Public Health / Department of Biochemistry / Stanford University / University of Washington / Seattle / National Center for Research Resources / Oxford University / American Society for Biochemistry / office of Basic Energy Sciences / /

Person

Adhesin Binding / V. Beskhlebnaya / V / T. A. Tabata / V / Ronald E. Stenkamp / David J. Evans / Steve L. Moseley / Cristina P. Van Loy / Tami Tabata / Susan Lea / Bosch Robien / Isolde Le Trong / Anh-Linh Bui / Carl F. Marrs / Mark Robien / Konstantin Korotkov / Ram Samudrala / Diane Capps / Evgeni V. Sokurenko / Natalia Korotkova / Veronika L. Chesnokova / Alain L. Servin / /

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Position

refined model for crystal form I. Fig / model for the fimbrial structure / Director / usher / /

Product

penicillin / ampicillin / chloramphenicol / /

ProvinceOrState

Washington / Michigan / /

PublishedMedium

Environmental Research / Microbiology / Molecular Biology / /

SportsLeague

Stanford University / /

Technology

Bioinformatics / directed Mutagenesis / sensor chips / cloning / research-grade sensor chip / comparative modeling protocol / double-subtraction protocol / crystallization / corrected using the double-subtraction protocol / /

URL

http /

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