THE PERFECTION OF PROTEIN CRYSTALS PROBED BY DIRECT RECORDING OF BRAGG REFLECTION PROFILES WITH A QUASI-PLANAR X-RAY WAVE

被引：83

作者：

FOURME, R

DUCRUIX, A

RIESKAUTT, M

CAPELLE, B

机构：

[1] UNIV PARIS SUD,STRUCT BIOL LAB,CNRS,F-91198 GIF SUR YVETTE,FRANCE

[2] UNIV PARIS 06,MINERAL & CRISTALLOG LAB,CNRS,F-75252 PARIS 05,FRANCE

[3] UNIV DENIS DIDEROT,MINERAL & CRISTALLOG LAB,CNRS,F-75252 PARIS 05,FRANCE

来源：

JOURNAL OF SYNCHROTRON RADIATION | 1995年 / 2卷

关键词：

PROTEIN CRYSTAL PERFECTION; CRYSTAL GROWTH; LYSOZYME; COLLAGENASE;

D O I：

10.1107/S0909049595003943

中图分类号：

TH7 [仪器、仪表];

学科分类号：

0804 ; 080401 ; 081102 ;

摘要：

Profiles of Bragg reflections from earth-grown crystals of lysozyme from hen egg-white and collagenase from Hypoderma lineatum were directly recorded with a quasi-planar X-ray wave. One crystal of each protein was chosen for a detailed investigation. Each sample is shown to consist of only a few (three and two, respectively) highly ordered domains, misoriented with respect to each other by a few are seconds. The smallest rocking widths were observed for the large domain of the collagenase sample (FWHM corrected for instrumental broadening: 0.0016 degrees for a strong reflection al 3 Angstrom resolution). With appropriate improvements, this method might become a quantitative tool for characterizing the perfection of crystals from biological macromolecules.

引用

页码：136 / 142

页数：7