Crystallization and characterization of two crystal forms of the B800–850 light-harvesting complex from Rhodopseudomonas acidophila strain 10050

MZ Papiz, AM Hawthornthwaite, RJ Cogdell… - Journal of molecular …, 1989 - Elsevier
MZ Papiz, AM Hawthornthwaite, RJ Cogdell, KJ Woolley, PA Wightman, LA Ferguson…
Journal of molecular biology, 1989Elsevier
Two different crystal forms of the B800–850-antenna complex from Rhodopseudomonas
acidophila strain 10050 have been grown. This complex is an integral membrane protein
and is isolated as an oligomeric assembly with a molecular weight of approximately 84 kDa.
This assembly contains six α/β apoprotein pairs, 18 molecules of bacteriochlorophyll a and
nine molecules of carotenoid. The first crystal form has dimensions unit cell a= b= 75· 8 A ̊,
c= 97· 5 A ̊ with the space group P4 and diffracts to a resolution of 12· 0 Å. The second …
Two different crystal forms of the B800–850-antenna complex from Rhodopseudomonas acidophila strain 10050 have been grown. This complex is an integral membrane protein and is isolated as an oligomeric assembly with a molecular weight of approximately 84 kDa. This assembly contains six α/β apoprotein pairs, 18 molecules of bacteriochlorophyll a and nine molecules of carotenoid. The first crystal form has dimensions unit cell a= b= 75· 8 A ̊, c= 97· 5 A ̊ with the space group P4 and diffracts to a resolution of 12· 0 Å. The second crystal form is rhombohedral with dimensions unit cell a= 121· 1 A ̊, α= 60°, space group R32 and diffracts to a resolution of 3· 5 Å. Native data have been processes in both cases, to an R merge value of 9· 0 to 11· 0%. The X-ray data suggest that the asymmetric unit, in both crystal forms, contains one 84 kDa antenna complex.
Elsevier
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