Double trouble - Buffer selection and his-tag presence may be responsible for nonreproducibility of biomedical experiments

Protein Science

Volumn 23, Issue 10, 2014, Pages 1359-1368

  Majorek, Karolina A ^a,b,c,d   Kuhn, Misty L ^d,e   Chruszcz, Maksymilian ^a,c,d,f   Anderson, Wayne F ^c,d,e   Minor, Wladek ^a,c,d  

^a UNIVERSITY OF VIRGINIA   (United States)

^b ADAM MICKIEWICZ UNIVERSITY   (Poland)

^c Midwest Center for Structural Genomics   (United States)

^d Center for Structural Genomics of Infectious Diseases (CSGID)   (United States)

^e NORTHWESTERN UNIVERSITY   (United States)

^f UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

acetyltransferase; GNAT; HEPES; His tag; polyhistidine affinity tag; reproducibility of biomedical experiments

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; ACYLTRANSFERASE; BACTERIAL PROTEIN; PA4794 PROTEIN; POLYHISTIDINE TAG; SACOL1063 ACETYLTRANSFERASE; SPERMIDINE; SPERMIDINE ACETYLTRANSFERASE; SPERMINE; SPERMINE ACETYLTRANSFERASE; UNCLASSIFIED DRUG; BUFFER; HISTIDINE; POLYHISTIDINE;

ARTICLE; BINDING SITE; BIOMEDICINE; COMPETITIVE INHIBITION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN ACETYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DETERMINATION; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA; REPRODUCIBILITY; STAPHYLOCOCCUS AUREUS; VIBRIO CHOLERAE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; MEDICAL RESEARCH; METABOLISM; MOLECULAR GENETICS; PROCEDURES; PROTEIN SECONDARY STRUCTURE;

PSEUDOMONAS AERUGINOSA;

ACETYLTRANSFERASES; BACTERIAL PROTEINS; BINDING SITES; BIOMEDICAL RESEARCH; BUFFERS; CATALYTIC DOMAIN; HISTIDINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA; REPRODUCIBILITY OF RESULTS;

EID: 84921764021     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2520     Document Type: Article

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