The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program

C. J. Gilmore; W. N. Nicholson; D. L. Dorset

doi:10.1107/s0108767396096468

The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program

C. J. Gilmore, W. N. Nicholson, D. L. Dorset

Research output: Contribution to journal › Article › peer-review

Abstract

Using the combination of maxirnum entropy and likelihood (Bricogne (1984) Acta Cryst. A40, 410-445) in the MICE computer program (Gilmore, Bricogne & Bannister (1990) Acta Cryst. A46, 297-308), an ab initio phase detem1ination was carried out at low resolution (6A) for two dissimilar membrane proteins, the Omp F porin from the outer membrane of E. coli (which is largely beta-sheet) and halorhodopsin (which is largely alphahelix)

Original language	English
Pages (from-to)	C65
Number of pages	1
Journal	Acta Crystallographica Section A: Foundations and Advances
Volume	52
Issue number	Suppl.
DOIs	https://doi.org/10.1107/s0108767396096468
Publication status	Published - 8 Aug 1996
Event	Seventeenth Congress and General Assembly of the International Union of Crystallography - Washington State Trade and Convention Center, Seattle, United States Duration: 8 Aug 1996 → 17 Aug 1996 https://www.iucr.org/iucr/cong/iucr-xvii

Access to Document

10.1107/s0108767396096468

Cite this

Gilmore, C. J., Nicholson, W. N., & Dorset, D. L. (1996). The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program. Acta Crystallographica Section A: Foundations and Advances, 52(Suppl.), C65. https://doi.org/10.1107/s0108767396096468

@article{c1cca6fa2c0043e09afb75dc1e199da1,

title = "The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 {\AA} from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program",

abstract = "Using the combination of maxirnum entropy and likelihood (Bricogne (1984) Acta Cryst. A40, 410-445) in the MICE computer program (Gilmore, Bricogne & Bannister (1990) Acta Cryst. A46, 297-308), an ab initio phase detem1ination was carried out at low resolution (6A) for two dissimilar membrane proteins, the Omp F porin from the outer membrane of E. coli (which is largely beta-sheet) and halorhodopsin (which is largely alphahelix)",

author = "Gilmore, {C. J.} and Nicholson, {W. N.} and Dorset, {D. L.}",

year = "1996",

month = aug,

day = "8",

doi = "10.1107/s0108767396096468",

language = "English",

volume = "52",

pages = "C65",

journal = "Acta Crystallographica Section A: Foundations and Advances",

issn = "2053-2733",

publisher = "Wiley",

number = "Suppl.",

note = "Seventeenth Congress and General Assembly of the International Union of Crystallography ; Conference date: 08-08-1996 Through 17-08-1996",

url = "https://www.iucr.org/iucr/cong/iucr-xvii",

}

Gilmore, CJ, Nicholson, WN & Dorset, DL 1996, 'The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program', Acta Crystallographica Section A: Foundations and Advances, vol. 52, no. Suppl., pp. C65. https://doi.org/10.1107/s0108767396096468

The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program. / Gilmore, C. J.; Nicholson, W. N.; Dorset, D. L.
In: Acta Crystallographica Section A: Foundations and Advances, Vol. 52, No. Suppl., 08.08.1996, p. C65.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program

AU - Gilmore, C. J.

AU - Nicholson, W. N.

AU - Dorset, D. L.

PY - 1996/8/8

Y1 - 1996/8/8

N2 - Using the combination of maxirnum entropy and likelihood (Bricogne (1984) Acta Cryst. A40, 410-445) in the MICE computer program (Gilmore, Bricogne & Bannister (1990) Acta Cryst. A46, 297-308), an ab initio phase detem1ination was carried out at low resolution (6A) for two dissimilar membrane proteins, the Omp F porin from the outer membrane of E. coli (which is largely beta-sheet) and halorhodopsin (which is largely alphahelix)

AB - Using the combination of maxirnum entropy and likelihood (Bricogne (1984) Acta Cryst. A40, 410-445) in the MICE computer program (Gilmore, Bricogne & Bannister (1990) Acta Cryst. A46, 297-308), an ab initio phase detem1ination was carried out at low resolution (6A) for two dissimilar membrane proteins, the Omp F porin from the outer membrane of E. coli (which is largely beta-sheet) and halorhodopsin (which is largely alphahelix)

U2 - 10.1107/s0108767396096468

DO - 10.1107/s0108767396096468

M3 - Article

SN - 2053-2733

VL - 52

SP - C65

JO - Acta Crystallographica Section A: Foundations and Advances

JF - Acta Crystallographica Section A: Foundations and Advances

IS - Suppl.

T2 - Seventeenth Congress and General Assembly of the International Union of Crystallography

Y2 - 8 August 1996 through 17 August 1996

ER -

The ab initio solution of the halorhodopsin and Omp F porin membrane proteins at 6 Å from electron diffraction projection data using the maximum entropy likelihood method in the MICE computer program

Abstract

Access to Document

Fingerprint

Cite this