Feasibility study for the measurement of a large set of triplet phases from a small protein

1999 ◽  
Vol 55 (7) ◽  
pp. 1320-1328 ◽  
Author(s):  
Edgar Weckert ◽  
Kerstin Hölzer ◽  
Klaus Schroer ◽  
Johannes Zellner ◽  
Kurt Hümmer
Keyword(s):  
Experimental Data ◽  
Egg White ◽  
Large Set ◽  
Hen Egg White Lysozyme ◽  
Small Protein ◽  
Egg White Lysozyme ◽  
Small Proteins ◽  
Tetragonal Form ◽  
Hen Egg White ◽  
Hen Egg

The feasibility of measuring a set of triplet phases large enough to solve the structure of a small protein has been evaluated. A total of about 850 triplet phases have been measured from the tetragonal form of hen egg-white lysozyme. From these triplet phases, about 750 single phases can be derived. The experimental details of these measurements as well as the results, the values of the measured triplet phases, are reported. Additional experimental data from other small proteins are also presented.

An X-ray study of the physiological-temperature form of hen egg-white lysozyme at 2 Å resolution

1983 ◽  
Vol 217 (1209) ◽  
pp. 471-489 ◽  
Keyword(s):  
High Temperature ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Final Model ◽  
Egg White Lysozyme ◽  
Isomorphous Replacement ◽  
Tetragonal Form ◽  
Hen Egg White ◽  
Mean Square Difference ◽  
Hen Egg

The structure of the high-temperature orthorhombic form of hen egg-white lysozyme has been determined at 2.0 Å resolution. Initial images of the molecule were obtained at 6.0 Å resolution both by double isomorphous replacement and by molecular replacement with use of the known structure of the room-temperature tetragonal lysozyme. The initial model thus obtained ( R = 0.52 at 6.0 Å) was refined first as a rigid body at 6.0 Å and then by restrained least squares at 2.5 Å and later at 2.0 Å resolution. The final model ( R = 0.23 at 2.0 Å) was compared with that of the tetragonal form: the structures are very similar with a root mean square difference in superimposed α-carbon coordinates of 0.46 Å. There are, however, differences which are caused by a crystal contact involving the upper part of this active site in the high-temperature orthorhombic form. Because of this, residues Trp 62 and Pro 70 are much better ordered than in the tetragonal form, where they are exposed to solvent. These differences can partly explain the difficulty of inhibitor-binding in high-temperature orthorhombic crystals, but do not seem to reflect the particular behaviour of lysozyme in solution at high temperature.

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

The inhibitory role of clioquinol in the fibrillation of hen egg white lysozyme

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Inhibitory Role ◽  
Hen Egg White ◽  
Hen Egg
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