Crystallization and preliminary X‐ray diffraction studies of intact EF‐Tu from Thermus aquaticus YT‐1

FEBS Letters

Betzel, Christian²  Dauter, Zbyszek²  Lippmann, Corinna¹  Erdmann, Volker A.¹  Wilson, Keith² 

[1] Institut für Biochemie, Freie Universität Berlin, Thielallee 63, D-1000 Berlin 33, Germany;EMBL Outstation Hamburg, c/o DESY, Notkestr. 85, D-2000 Hamburg 52, FRG

关键词: Crystallization;    X-ray diffraction;    Synchrotron radiation;    Elongation factor Tu;   

DOI  :  10.1016/0014-5793(88)80355-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Many attempts have been made to elucidate the three-dimensional structure from elongation factor Tu, but so far the only crystals suitable for X-ray crystallography contained a partially degraded protein. Here, we report the crystallization of a fully active, intact EF-Tu from Thermus aquaticus. The crystals belong to hexagonal space group P6₃22 and diffract up to 2.6 Å. The cell dimensions are a = b = 178 Å, c = 238 Å and 6 molecules are contained per asymmetric unit.

【 授权许可】

Unknown