Electronic Reprint Structural Biology and Crystallization Communications Production, Purification and Preliminary X-ray Crystallographic Studies of Adeno-associated Virus Serotype 7 Structural Biology and Crystallization Communications Production, Purification and Preliminary X-ray Crystallographic
Electronic Reprint Structural Biology and Crystallization Communications Production, Purification and Preliminary X-ray Crystallographic Studies of Adeno-associated Virus Serotype 7 Structural Biology and Crystallization Communications Production, Purification and Preliminary X-ray Crystallographic
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Acta Crystallographica Section;H. M. Einspahr;J. M. Guss;O. Quesada;Brittney L. Gurda;L. Govindasamy;R. McKenna;E. Kohlbrenner;G. Aslanidi;S. Zolotukhin;N. Muzyczka;M. Agbandje-McKenna
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Acta Crystallographica Section;H. M. Einspahr;J. M. Guss;O. Quesada;Brittney L. Gurda;L. Govindasamy;R. McKenna;E. Kohlbrenner;G. Aslanidi;S. Zolotukhin;N. Muzyczka;M. Agbandje-McKenna
本文作者可在保留本封面页的前提下，将转载本文件载入自己的网站或机构资料库。未经IUCr事先书面许可，不得转载本文或将其存储在电子数据库中。杆状病毒表达的腺相关病毒血清型7衣壳的晶体使X射线的分辨率达到3.0美元。晶体属于菱面体空间群R3，六方晶系晶胞参数a = 252.4，c = 591.2 A.处理衍射数据并将其简化为79.0%的总体完整性和12.0%的R合并。在单位细胞中有三个病毒衣壳。二十面体三重轴与晶体学三重轴重合，导致每个晶体学不对称单元有三分之一的衣壳（20个单体）。病毒衣壳的方向已通过旋转函数搜索确定，并通过包装考虑定位在（0，0，0）。
Author(s) of this paper may load this reprint on their own web site or institutional repository provided that this cover page is retained. Republication of this article or its storage in electronic databases other than as specified above is not permitted without prior permission in writing from the IUCr. Crystals of baculovirus-expressed adeno-associated virus serotype 7 capsids diffract X-rays to $3.0 A ˚ resolution. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = 252.4, c = 591.2 A ˚ in the hexagonal setting. The diffraction data were processed and reduced to an overall completeness of 79.0% and an R merge of 12.0%. There are three viral capsids in the unit cell. The icosahedral threefold axis is coincident with the crystallographic threefold axis, resulting in one third of a capsid (20 monomers) per crystallographic asymmetric unit. The orientation of the viral capsid has been determined by rotation-function searches and is positioned at (0, 0, 0) by packing considerations.