Abstract
Cytochrome c2 from Rhodobacter sphaeroides, which serves as the secondary donor in bacterial photosynthesis, has been crystallized from ammonium sulfate solutions at pH 7.0 by vapor diffusion. The crystals are well formed with clearly discernable facets. Their space group is P6522 (or its enantiomorph P6122) with unit cell dimensions a = b = 64.5 A ̊ and c = 163.0 A ̊, and two proteins per asymmetric unit. The crystals diffract to at least 2.7 Å and are stable during X-ray exposure for several days.
Original language | English |
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Pages (from-to) | 495-496 |
Number of pages | 2 |
Journal | Journal of Molecular Biology |
Volume | 204 |
Issue number | 2 |
DOIs | |
Publication status | Published - Nov 20 1988 |
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ASJC Scopus subject areas
- Virology
Cite this
Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides. / Allen, James Paul.
In: Journal of Molecular Biology, Vol. 204, No. 2, 20.11.1988, p. 495-496.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides
AU - Allen, James Paul
PY - 1988/11/20
Y1 - 1988/11/20
N2 - Cytochrome c2 from Rhodobacter sphaeroides, which serves as the secondary donor in bacterial photosynthesis, has been crystallized from ammonium sulfate solutions at pH 7.0 by vapor diffusion. The crystals are well formed with clearly discernable facets. Their space group is P6522 (or its enantiomorph P6122) with unit cell dimensions a = b = 64.5 A ̊ and c = 163.0 A ̊, and two proteins per asymmetric unit. The crystals diffract to at least 2.7 Å and are stable during X-ray exposure for several days.
AB - Cytochrome c2 from Rhodobacter sphaeroides, which serves as the secondary donor in bacterial photosynthesis, has been crystallized from ammonium sulfate solutions at pH 7.0 by vapor diffusion. The crystals are well formed with clearly discernable facets. Their space group is P6522 (or its enantiomorph P6122) with unit cell dimensions a = b = 64.5 A ̊ and c = 163.0 A ̊, and two proteins per asymmetric unit. The crystals diffract to at least 2.7 Å and are stable during X-ray exposure for several days.
UR - http://www.scopus.com/inward/record.url?scp=0024293460&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024293460&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(88)90592-X
DO - 10.1016/0022-2836(88)90592-X
M3 - Article
C2 - 2851662
AN - SCOPUS:0024293460
VL - 204
SP - 495
EP - 496
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 2
ER -