1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
复制标题
1.59 120 K 下胰蛋白酶的结构：低温和室温结构的比较。
DOI：
10.1002/prot.340100303
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Stroud,R
中科院分区：
文献类型：
--
作者：
Earnest,T;Fauman,E;Craik,CS;Stroud,R
The structure of a rat trypsin mutant [S195C] at a temperature of 120 K has been refined to a crystallographicRfactor of 17.4% between 12.0 and 1.59 Å and is compared with the structure of the D102N mutant at 295 K. A reduction in the unit cell dimensions in going from room temperature to low temperature is accompanied by a decrease in molecular surface area and radius of gyration. The overall structure remains similar to that at room temperature. The attainable resolution appears to be improved due to the decrease in the fall off of intensities with resolution [reduction of the temperature factor]. This decreases the uncertainty in the atomic positions and allows the localization of more protein atoms and solvent molecules in the low temperature map. The largest differences between the two models occur at residues with higher than average temperature factors. Several features can be localized in the solvent region of the 120 K map that are not seen in the 295 K map. These include several more water molecules as well as an interstitial sulfate ion and two interstitial benzamidine molecules.
