Crystallization and preliminary X-ray diffraction studies of coxsackievirus B1

Thomas Li; Anqiang Zhang; Narushi Iizuka; Akio Nomoto; Edward Arnold

doi:10.1016/0022-2836(92)90268-O

Crystallization and preliminary X-ray diffraction studies of coxsackievirus B1

Thomas Li, Anqiang Zhang, Narushi Iizuka, Akio Nomoto, Edward Arnold

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

4 Citations (Scopus)

Abstract

Preparations of coxsackievirus B1 (CVB1) derived from an infectious cDNA clone have been crystallized in multiple crystal forms. Using high intensity synchrotron radiation, an orthorhombic form of the crystals was shown to diffract X-rays to at least 2.9 Å resolution. The unit cell has a primitive lattice with dimensions a = 323 A ̊, b = 450 A ̊, and c = 522 A ̊. A crystallographic asymmetric unit of these CVB1 crystals probably contains an entire virus particle, implying the presence of 60-fold non-crystallographic redundancy. This CVB1 crystal form appears to be suitable for high-resolution structure determination by X-ray crystallography.

Original language	English
Pages (from-to)	1171-1175
Number of pages	5
Journal	Journal of Molecular Biology
Volume	223
Issue number	4
DOIs	https://doi.org/10.1016/0022-2836(92)90268-O
Publication status	Published - 20-02-1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

Access to Document

10.1016/0022-2836(92)90268-O

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title = "Crystallization and preliminary X-ray diffraction studies of coxsackievirus B1",

abstract = "Preparations of coxsackievirus B1 (CVB1) derived from an infectious cDNA clone have been crystallized in multiple crystal forms. Using high intensity synchrotron radiation, an orthorhombic form of the crystals was shown to diffract X-rays to at least 2.9 {\AA} resolution. The unit cell has a primitive lattice with dimensions a = 323 A ̊, b = 450 A ̊, and c = 522 A ̊. A crystallographic asymmetric unit of these CVB1 crystals probably contains an entire virus particle, implying the presence of 60-fold non-crystallographic redundancy. This CVB1 crystal form appears to be suitable for high-resolution structure determination by X-ray crystallography.",

author = "Thomas Li and Anqiang Zhang and Narushi Iizuka and Akio Nomoto and Edward Arnold",

year = "1992",

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doi = "10.1016/0022-2836(92)90268-O",

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T1 - Crystallization and preliminary X-ray diffraction studies of coxsackievirus B1

AU - Li, Thomas

AU - Zhang, Anqiang

AU - Iizuka, Narushi

AU - Nomoto, Akio

AU - Arnold, Edward

PY - 1992/2/20

Y1 - 1992/2/20

N2 - Preparations of coxsackievirus B1 (CVB1) derived from an infectious cDNA clone have been crystallized in multiple crystal forms. Using high intensity synchrotron radiation, an orthorhombic form of the crystals was shown to diffract X-rays to at least 2.9 Å resolution. The unit cell has a primitive lattice with dimensions a = 323 A ̊, b = 450 A ̊, and c = 522 A ̊. A crystallographic asymmetric unit of these CVB1 crystals probably contains an entire virus particle, implying the presence of 60-fold non-crystallographic redundancy. This CVB1 crystal form appears to be suitable for high-resolution structure determination by X-ray crystallography.

AB - Preparations of coxsackievirus B1 (CVB1) derived from an infectious cDNA clone have been crystallized in multiple crystal forms. Using high intensity synchrotron radiation, an orthorhombic form of the crystals was shown to diffract X-rays to at least 2.9 Å resolution. The unit cell has a primitive lattice with dimensions a = 323 A ̊, b = 450 A ̊, and c = 522 A ̊. A crystallographic asymmetric unit of these CVB1 crystals probably contains an entire virus particle, implying the presence of 60-fold non-crystallographic redundancy. This CVB1 crystal form appears to be suitable for high-resolution structure determination by X-ray crystallography.

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