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Volumn 272, Issue 5264, 1996, Pages 1001-1004

Structures of an MHC class II molecule with covalently bound single peptides

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; T LYMPHOCYTE RECEPTOR;

EID: 0029782111     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5264.1001     Document Type: Article
Times cited : (337)

References (34)
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    • k-Hsp of data collection quality by equilibrating 5 to 10 mg/ml of purified protein against 16 to 18% polyethylene glycol 4000 (Fluka), 2% ethylene glycol, 200 mM ammonium sulfate, and 100 mM citrate (pH 5.2 to 5.6). Crystals were cryoprotected by the addition of 20% polyethylene glycol 4000, 20% ethylene glycol, and 10% glycerol.
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    • note
    • sym = 0.087 and 92.1% completion between 20 and 2.7 A The solvent contents are 55% and 60% for the respective crystals with two heterodimeric complexes per asymmetric unit.
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    • note
    • kHb crystal. Perhaps dimer packing in the different space groups, slight differences in pH, or small changes in the dimer interface controlled the sequestering of the sulfate ion. There is no obvious influence of the peptide or linker on sulfate coordination.
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    • note
    • We thank J. Clements, F. Crawford, H. Kozono, D. Parker, and J. White for help in making the soluble class II molecules and H.-E. Aronson, K. Choi, C. Lima, X. Zhao, and X. Zhu for aid in the synchrotron data collection and Nir Ben-Tal for electrostatic discussions. Coordinates have been deposited in the Brookhaven Protein Data Bank (entries 1IEA and 1IEB) and are available via e-mail (fremont@ columbia.edu).


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