TY - JOUR
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
N1 - Funding Information:
and Gail Ferstandig Arnold for their support, in having the appropriate local facilities for handling CVBl samples and for their interest in the work. We thank Iku Ise for help in preparation of HeLa S3 cells; Jeff White for help in arranging safety precautions at CHESS for this project; Jorge Lopez at the Cornell Virus Diagnostic Laboratory for access to a biological safety cabinet for crystal mounting; and Donald Bilderback and the entire CHESS staff for their support of our experiments and for continuing development of the Ma&HESS facility. Nagi Ayad, Alfred0 Jaeobo-Molina, Raymond Nanni, Deena Oren, Dawn Rubenstein and Roger Williams are grate- fully acknowledged for their help in data collection at CHESS. We thank Edward Rozhon, Stu Cox and John O’Connell for useful discussions about coxsackieviruses. We are also grateful to Richard L. Crowell and Barbara Alstein for testing our laboratory members’ blood samples for evidence of prior coxsackievirus infection and for helpful discussions. Support for this project to E.A. has been provided by the Center for Advanced Biotechnology and Medicine and the New Jersey Commission on Science and Technology, and to A.N. by research grants from the Ministry of Education, Science and Culture of Japan. E.A. is an Alfred P. Sloan Foundation Research Fellow,
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.
UR - https://www.scopus.com/pages/publications/0026533813
UR - https://www.scopus.com/pages/publications/0026533813#tab=citedBy
U2 - 10.1016/0022-2836(92)90268-O
DO - 10.1016/0022-2836(92)90268-O
M3 - Article
C2 - 1311388
AN - SCOPUS:0026533813
SN - 0022-2836
VL - 223
SP - 1171
EP - 1175
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 4
ER -