Abstract
The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 Å and c = 276.7 Å with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 Å consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement.
| Original language | English |
|---|---|
| Pages (from-to) | 283-286 |
| Number of pages | 4 |
| Journal | Proteins: Structure, Function and Bioinformatics |
| Volume | 20 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1994 |
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Keywords
- detergent
- membrane protein
- photosynthesis
- pigment- protein complexes
- protein structure
ASJC Scopus subject areas
- Genetics
- Structural Biology
- Biochemistry
Cite this
Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form. / Allen, James Paul.
In: Proteins: Structure, Function and Bioinformatics, Vol. 20, No. 3, 1994, p. 283-286.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form
AU - Allen, James Paul
PY - 1994
Y1 - 1994
N2 - The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 Å and c = 276.7 Å with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 Å consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement.
AB - The reaction center from the nonsulfur purple bacterium Rhodobacter sphaeroides has been crystallized in a new form. The crystals grew in the presence of polyethylene glycol 4000, the detergent β-octyl glucoside, and the amphiphiles heptane triol and benzamidine hydrochloride, using the sitting drop method. The space group of these crystals is tetragonal, P41(43)212, and the cell constants are a = b = 141.5 Å and c = 276.7 Å with probably 2 proteins per asymmetric unit. A native data set has been set collected to a resolution of 2.8 Å consisting of 56,332 unique reflections (50,731 with F>2σ) with an R(sym) of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement.
KW - detergent
KW - membrane protein
KW - photosynthesis
KW - pigment- protein complexes
KW - protein structure
UR - http://www.scopus.com/inward/record.url?scp=0027973329&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027973329&partnerID=8YFLogxK
U2 - 10.1002/prot.340200309
DO - 10.1002/prot.340200309
M3 - Article
C2 - 7892177
AN - SCOPUS:0027973329
VL - 20
SP - 283
EP - 286
JO - Proteins: Structure, Function and Genetics
JF - Proteins: Structure, Function and Genetics
SN - 0887-3585
IS - 3
ER -