Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
SAD (single-wavelength anomalous diffraction) has enormous potential for phasing proteins using only the anomalous signal of the almost ubiquitous native sulfur, but requires extremely precise data. The previously unknown structure of the lima bean trypsin inhibitor (LBTI) was solved using highly redundant data collected to 3 A using a CCD detector with a rotating-anode generator and three-circle goniometer. The seven 'super-S' atoms (disulfide bridges) were located by dual-space recycling with SHELXD and the high solvent content enabled the density-modification program SHELXE to generate high-quality maps despite the modest resolution. Subsequently, a 2.05 A synchrotron data set was collected and used for further phase extension and structure refinement.
In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case.,Debreczeni JE, Bunkoczi G, Girmann B, Sheldrick GM Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):393-5. Epub 2003, Jan 23. PMID:12554963[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Debreczeni JE, Bunkoczi G, Girmann B, Sheldrick GM. In-house phase determination of the lima bean trypsin inhibitor: a low-resolution sulfur-SAD case. Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):393-5. Epub 2003, Jan 23. PMID:12554963
