3NIR

Crystal structure of small protein crambin at 0.48 A resolution

Summary for 3NIR

• Entry DOI: 10.2210/pdb3nir/pdb
• Related: 1AB1 1CBN 1CNR 1CRN 1EJG
• Descriptor: Crambin, ETHANOL (3 entities in total)
• Functional Keywords: plant protein
• Biological source: Crambe hispanica (Abyssinian crambe, Abyssinian kale)
• Cellular location: Secreted: P01542
• Total number of polymer chains: 1
• Total formula weight: 4922.72

Authors

Schmidt, A.,Teeter, M.,Weckert, E.,Lamzin, V.S. (deposition date: 2010-06-16, release date: 2011-05-18, Last modification date: 2024-11-20)

Primary citation

Schmidt, A.,Teeter, M.,Weckert, E.,Lamzin, V.S.
Crystal structure of small protein crambin at 0.48 A resolution
Acta Crystallogr.,Sect.F, 67:424-429, 2011

PubMed Abstract: With the development of highly brilliant and extremely intense synchrotron X-ray sources, extreme high-resolution limits for biological samples are now becoming attainable. Here, a study is presented that sets the record in crystallographic resolution for a biological macromolecule. The structure of the small protein crambin was determined to 0.48 Å resolution on the PETRA II ring before its conversion to a dedicated synchrotron-radiation source. The results reveal a wealth of details in electron density and demonstrate the possibilities that are potentially offered by a high-energy source. The question now arises as to what the true limits are in terms of what can be seen at such high resolution. From what can be extrapolated from the results using crystals of crambin, this limit would be at approximately 0.40 Å, which approaches that for smaller compounds.

PubMed: 21505232
DOI: 10.1107/S1744309110052607

Experimental method

X-RAY DIFFRACTION (0.48 Å)