Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BWE

Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity

Summary for 4BWE
Entry DOI10.2210/pdb4bwe/pdb
DescriptorGlypican-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordsmembrane protein, proteoglycan, glycosaminoglycans, heparan sulfate, glycoprotein, helical bundle
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight216104.95
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 citationAwad, 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: 24311593
DOI: 10.1107/S0907444913025250
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.46 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon