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Crystal structure of catechol O-methyltransferase
CATECHOL O-methyltransferase (COMT, EC is important in the central nervous system because it metabolizes catecholamine neurotransmitters such as dopamine. The enzyme catalyses the transferExpand
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Three‐dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 × 60 × 118 A. The GTPExpand
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Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.
In order to obtain a better structural framework for understanding the catalytic mechanism of carbonic anhydrase, a number of inhibitor complexes of the enzyme were investigated crystallographically.Expand
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The crystallography beamline I711 at MAX II.
A new X-ray crystallographic beamline is operational at the MAX II synchrotron in Lund. The beamline has been in regular use since August 1998 and is used both for macro- and small moleculeExpand
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Structure of phosphate-free ribonuclease A refined at 1.26 A.
The structure of phosphate-free bovine ribonuclease A has been refined at 1.26-A resolution by a restrained least-squares procedure to a final R factor of 0.15. X-ray diffraction data were collectedExpand
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Crystal structure of the superantigen staphylococcal enterotoxin type A.
Staphylococcal enterotoxins are prototype superantigens characterized by their ability to bind to major histocompatibility complex (MHC) class II molecules and subsequently activate a large fractionExpand
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Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography.
In a structure of recombinant bovine calbindin D9k, determined crystallographically to 1.6 A resolution, a proline in mixed, approximately equally populated, cis and trans conformation is observed.Expand
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Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
The three‐dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA‐DR1) has been determined byExpand
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The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules.
The X-ray structure of the superantigen staphylococcal enterotoxin H (SEH) has been determined at 1.69 A resolution. In this paper we present two structures of zinc-free SEH (apoSEH) and oneExpand
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A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity.
Staphylococcal enterotoxins and toxic shock syndrome toxin-1 are known as superantigens due to their ability to activate a large number of T-cells by crosslinking the major histocompatibility complexExpand
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