On the use of DXMS to produce more crystallizable proteins: Structures of the T. maritima proteins TM0160 and TM1171

Protein Science

Volumn 13, Issue 12, 2004, Pages 3187-3199

  Spraggon, Glen ^a   Pantazatos, Dennis ^b   Klock, Heath E ^a   Wilson, Ian A ^c   Woods Jr , Virgil L ^b   Lesley, Scott A ^a  

^a GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION   (United States)

^b UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Crystallization; Mass spectrometry; Novel fold; Protein structure; Sequence complexity

Indexed keywords

AMIDE; BACTERIAL PROTEIN; DEUTERIUM; PROTEIN TM0160; PROTEIN TM1171; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENOME; CRYSTAL STRUCTURE; CRYSTALLIZATION; DUETERIUM EXCHANGE MASS SPECTROSCOPY; HYPOTHESIS; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THERMOTOGA MARITIMA;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; GENOME; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE DELETION; THERMOTOGA MARITIMA;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 9344256689     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04939904     Document Type: Article

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