Abstract
The reaction center from the nonsulfur purple bacteriumRhodobacter sphaeroideshas 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 anRsym of 9.5%. Analysis of the diffraction data is underway using molecular and isomorphous replacement. © 1994 Wiley‐Liss, Inc.
Original language | English |
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Pages (from-to) | 283-286 |
Number of pages | 4 |
Journal | Proteins: Structure, Function, and Bioinformatics |
Volume | 20 |
Issue number | 3 |
DOIs | |
Publication status | Published - Nov 1994 |
Keywords
- detergent
- membrane protein
- photosynthesis
- pigment‐protein complexes
- protein structure
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology