The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A Λresolution. This hexagonal crystal form crystallizes from a saturated sodium nitrate solution at pH 8.4. The crystals belong to space group P6 1 22, with unit-cell
Crystallography of succinimide hen egg-white lysozyme at low temperatures
β Scribed by Kazuki Miyawaki; Shuji Noguchi; Shigeharu Harada; Yoshinori Satow
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 322 KB
- Volume
- 168
- Category
- Article
- ISSN
- 0022-0248
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Water loss during lyophilization of a 49.4 mg/mL solution of lysozyme in D,O was studied with ir spectroscopy using a low-temperature, single reflection, horizontal, attenuated, total reflectance accessory. Four regions of water loss were identified and assignable to different forms of bound water.
Electrosynthesis provides a novel methodology to produce specific and selective chemical reaction in proteins. Thus electrooxidation of hen egg-white lysozyme (HEWL) at + 1.2 V (vs see) at a carbon anode in mildly acid buffer produces selective oxidation at methionine-105; while by increase in anodi
## Abstract Metal binding to lysozyme has recieved wide interest. In particular, it is interesting that Ni^2+^, Mn^2+^, Co^2+^, and Yb^3+^ chloride salts induce an increase in the solubility of the tetragonal form in crystals of hen egg white lysozyme at high salt concentration, but that Mg^2+^ and