IUCr journals

Crystal structure of small protein crambin at 0.48 Å resolution

Acta Cryst. (2011). F67, 424-428 (doi.org/10.1107/S1744309110052607)

[Crambin] Electron density (cyan) around Arg10 calculated at 0.65 Å before refinement with MoPro commenced. The FoFc map is contoured at 2.7σ (0.25 e Å−3) above the mean. Bonding electron density is indicated.

Scientists at EMBL and DESY, Germany, and Boston College, USA, obtained the highest resolution X-ray crystallographic structure of a biological molecule, crambin, almost doubling the available data on this protein. The researchers hope that the availability of this data will drive software development beyond its current limits so that details of protein electronic structure could become attainable. This high-resolution structure was the first measured at the PETRA ring at DESY, where dedicated beamlines for biological samples are coming into operation.

A. Schmidt, M. Teeter, E. Weckert and V. S. Lamzin