1PS5

STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION

1PS5 の概要

• エントリーDOI: 10.2210/pdb1ps5/pdb
• 分子名称: Lysozyme C, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, glycosidase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14523.29

構造登録者

Majeed, S.,Ofek, G.,Belachew, A.,Huang, C.,Zhou, T.,Kwong, P.D. (登録日: 2003-06-20, 公開日: 2003-09-09, 最終更新日: 2024-11-06)

主引用文献

Majeed, S.,Ofek, G.,Belachew, A.,Huang, C.,Zhou, T.,Kwong, P.D.
Enhancing Protein Crystallization through Precipitant Synergy
Structure, 11:1061-1070, 2003

PubMed Abstract: Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization.

PubMed: 12962625
DOI: 10.1016/S0969-2126(03)00185-0

実験手法

X-RAY DIFFRACTION (2 Å)