Comparison of structures of dry and wet hen egg‐white lysozyme molecule at 1.8 Å resolution

FEBS Letters

Nekrasov, Yu.V.¹  Vagin, A.A.¹  Kachalova, G.S.²  Morozov, V.N.²  Morozova, T.Ya.²  Myachin, E.T.²  Strokopytov, B.V.¹ 

[1] Institute of Crystallography of the Academy of Sciences of the USSR, Leninsky Prospect 59, Moscow, USSR 117333;Institute of Biological Physics of the Academy of Sciences of the USSR, Pushchino, Moscow Region, USSR 142292

关键词: Dehydration;    Protein structure;    Lysozyme;    X-ray diffraction;   

DOI  :  10.1016/0014-5793(91)80769-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A high resolution structure of hen egg-white lysozyme containing 36 ± I mol H₂O per mol of protein has been obtained using triclinic (P₁) crystals cross-linked with glutaraldehyde. Analysis of dehydration-induced structural changes has revealed displacement in relative position of domains and numerous small displacements in positions of individual atoms with r.m.s. deviation of main atoms 0.60 Å, and that of all atoms 0.97 Å. An increase in the average packing density of atoms in dry lysozyme by 4–6% seems to be the most probable reason for the loss of its activity and mobility.

【 授权许可】

Unknown