4TPL

West Nile Virus Non-structural protein 1 (NS1) Form 1 crystal

4TPL の概要

• エントリーDOI: 10.2210/pdb4tpl/pdb
• 分子名称: West Nile Virus NS1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: flavivirus, non-structural protein 1, ns1, viral protein
• 由来する生物種: West Nile virus (WNV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90313.99

構造登録者

Akey, D.L.,Smith, J.L. (登録日: 2014-06-08, 公開日: 2014-10-15, 最終更新日: 2023-12-27)

主引用文献

Akey, D.L.,Brown, W.C.,Konwerski, J.R.,Ogata, C.M.,Smith, J.L.
Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1.
Acta Crystallogr.,Sect.D, 70:2719-2729, 2014

PubMed Abstract: An emergent challenge in macromolecular crystallography is the identification of the substructure from native anomalous scatterers in crystals that diffract to low to moderate resolution. Increasing the multiplicity of data sets has been shown to make previously intractable phasing problems solvable and to increase the useful resolution in model refinement. For the West Nile virus nonstructural protein 1 (NS1), a protein of novel fold, the utility of exceptionally high multiplicity data is demonstrated both in solving the crystal structure from the anomalous scattering of the native S atoms and in extending the useful limits of resolution during refinement. A high-multiplicity data set from 18 crystals had sufficient anomalous signal to identify sulfur sites using data to 5.2 Å resolution. Phases calculated to 4.5 Å resolution and extended to 3.0 Å resolution were of sufficient quality for automated building of three-quarters of the final structure. Crystallographic refinement to 2.9 Å resolution proceeded smoothly, justifying the increase in resolution that was made possible by combining multiple data sets. The identification and exclusion of data from outlier crystals is shown to result in more robust substructure determination.

PubMed: 25286855
DOI: 10.1107/S1399004714017556

実験手法

X-RAY DIFFRACTION (2.9 Å)