Electron crystallography of PhoE porin, an outer membrane, channel- forming protein from E. coli

Technical Report · Wed Nov 01 00:00:00 EST 1989

DOI:https://doi.org/10.2172/6365889· OSTI ID:6365889

Walian, P J

One approach to studying the structure of membrane proteins is the use of electron crystallography. Dr. Bing Jap has crystallized PhoE pore-forming protein (porin) from the outer membrane of escherichia coli (E. coli) into monolayer crystals. The findings of this research and those of Jap (1988, 1989) have determined these crystals to be highly ordered, yielding structural information to a resolution of better than 2.8 angstroms. The task of this thesis has been to collect and process the electron diffraction patterns necessary to generate a complete three-dimensional set of high resolution structure factor amplitudes of PhoE porin. Fourier processing of these amplitudes when combined with the corresponding phase data is expected to yield the three-dimensional structure of PhoE porin at better than 3.5 angstroms resolution. 92 refs., 33 figs., 3 tabs. (CBS)

• Research Organization: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
• Sponsoring Organization: DOE/ER; DOHHS
• DOE Contract Number: AC03-76SF00098
• OSTI ID: 6365889
• Report Number(s): LBL-28625; ON: DE91001790; CNN: GM36884
• Resource Relation: Other Information: Thesis (Ph.D.)
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ESCHERICHIA COLI
MEMBRANE TRANSPORT
PORINS
PROTEIN STRUCTURE
CRYSTALLOGRAPHY
CRYSTALS
ELECTRON DIFFRACTION
ELECTRON MICROSCOPY
FOURIER ANALYSIS
MEMBRANE PROTEINS
MEMBRANES
STRUCTURAL CHEMICAL ANALYSIS
BACTERIA
COHERENT SCATTERING
DIFFRACTION
MICROORGANISMS
MICROSCOPY
ORGANIC COMPOUNDS
PROTEINS
SCATTERING
550700* - Microbiology
550200 - Biochemistry