Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides

James Paul Allen

doi:10.1016/0022-2836(88)90592-X

Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides

James Paul Allen

Arizona State University

Research output: Contribution to journal › Article

3 Citations (Scopus)

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
Pages (from-to)	495-496
Number of pages	2
Journal	Journal of Molecular Biology
Volume	204
Issue number	2
DOIs	https://doi.org/10.1016/0022-2836(88)90592-X
Publication status	Published - Nov 20 1988

ASJC Scopus subject areas

Virology

Access to Document

10.1016/0022-2836(88)90592-X

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides'. Together they form a unique fingerprint.

Cite this

Allen, J. P. (1988). Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides. Journal of Molecular Biology, 204(2), 495-496. https://doi.org/10.1016/0022-2836(88)90592-X

@article{3b803040730a483088811fea6097ebe7,

title = "Crystallization and preliminary X-ray diffraction analysis of cytochrome c2 from Rhodobacter sphaeroides",

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 {\AA} and are stable during X-ray exposure for several days.",

author = "Allen, {James Paul}",

year = "1988",

month = nov,

day = "20",

doi = "10.1016/0022-2836(88)90592-X",

language = "English",

volume = "204",

pages = "495--496",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

number = "2",

}

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 -