4BWE
Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
Summary for 4BWE
Entry DOI | 10.2210/pdb4bwe/pdb |
Descriptor | Glypican-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | membrane protein, proteoglycan, glycosaminoglycans, heparan sulfate, glycoprotein, helical bundle |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 4 |
Total formula weight | 216104.95 |
Authors | Awad, W.,Svensson Birkedal, G.,Thunnissen, M.M.G.M.,Mani, K.,Logan, D.T. (deposition date: 2013-07-01, release date: 2013-12-18, Last modification date: 2023-12-20) |
Primary citation | Awad, W.,Svensson Birkedal, G.,Thunnissen, M.M.,Mani, K.,Logan, D.T. Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration. Acta Crystallogr. D Biol. Crystallogr., 69:2524-2533, 2013 Cited by PubMed Abstract: The use of controlled dehydration for improvement of protein crystal diffraction quality is increasing in popularity, although there are still relatively few documented examples of success. A study has been carried out to establish whether controlled dehydration could be used to improve the anisotropy of crystals of the core protein of the human proteoglycan glypican-1. Crystals were subjected to controlled dehydration using the HC1 device. The optimal protocol for dehydration was developed by careful investigation of the following parameters: dehydration rate, final relative humidity and total incubation time Tinc. Of these, the most important was shown to be Tinc. After dehydration using the optimal protocol the crystals showed significantly reduced anisotropy and improved electron density, allowing the building of previously disordered parts of the structure. PubMed: 24311593DOI: 10.1107/S0907444913025250 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.46 Å) |
Structure validation
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