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Hemoglobin / Histidine / Chemistry / Histidine decarboxylase / Enzyme


PROTEINS: Structure, Function, and Genetics 46:321–[removed]DOI[removed]prot[removed]Structure and Cooperativity of a T-State Mutant of Histidine Decarboxylase From Lactobacillus 30a Scott Worley, Elisabeth Schelp, Art
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Document Date: 2005-01-04 12:23:48


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City

Recsei / Niguel / St. Louis / /

Company

Sigma Chemical Co. / Protein Data Bank / Wiley-Liss Inc. / Yale University Press / Patterson / Silicon Graphics / Urzhumtsev AG / I4122 / C2221 / /

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Event

FDA Phase / /

Facility

terminal S81 / Welch Hall / University of Texas / HME complex / Jon D. Robertus* Institute of Cellular / Model building / /

IndustryTerm

active site / substrate-binding site / imidazole-binding site / pyruvoyl / cryoprotectant solution / adjacent active site / slow cooling protocol / disorganized active site / free energy differences / given local active site / precipitant solution / space / /

Organization

Foundation for Research / Jon D. Robertus* Institute of Cellular and Molecular Biology / C. This / National Science Foundation / Department of Chemistry and Biochemistry / Welch Foundation / Yale University / University of Texas / /

Person

Elisabeth Schelp / Scott Worley / Arthur F. Monzingo / Jon D. Robertus / Stephen Ernst / Ernst SR / Austin Texas / /

Position

RT / Butler / /

Product

MAPMAN22 / sodium acetate / X-PLOR / /

ProvinceOrState

Alabama / Copeland / Laguna / HDC / /

PublishedMedium

Molecular Biology / /

Technology

X-ray / directed mutagenesis / Crystallization / flash / slow cooling protocol / /

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