𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Structure of oxy- and deoxy-erythrocruorin at 1.4 Å resolution

✍ Scribed by W. Steigemann; E. Weber

Publisher
Springer
Year
1980
Tongue
English
Weight
72 KB
Volume
6
Category
Article
ISSN
1432-1017

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Crystal structure of 1-deoxy-d-xylulose-
Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase from Zymomonas mobilis at 1.9-Å resolution
✍ Stefano Ricagno; Sigrid Grolle; Stephanie Bringer-Meyer; Hermann Sahm; Ylva Lind 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 864 KB

1-Deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A ˚resolution, and that of a binary complex with the co-substrat

Structure of Paramecium tetraurelia calm
Structure of Paramecium tetraurelia calmodulin at 1.8 Å resolution
✍ S. T. Rao; S. Wu; K. A. Satyshur; M. Sundaralingam; K.-Y. Ling; C. Kung 📂 Article 📅 2008 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 1022 KB

## Abstract The crystal structure of calmodulin (CaM; __M__~r~ 16, 700, 148 residues) from the ciliated protozoan __Paramecium tetraurelia__ (PCaM) has been determined and refined using 1.8 Å resolution area detector data. The crystals are triclinic, space group P1, __a__ = 29.66, __b__ = 53.79, __

Structure and function of chromophores i
Structure and function of chromophores in R-phycoerythrin at 1.9 Å resolution
✍ Tao Jiang; Ji-ping Zhang; Dong-cai Liang 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 260 KB

The crystal structure of R-Phycoerythrin (R-PE) from Polysiphonia urceolata has been refined to a resolution of 1.9 Å, based on the atomic coordinates of R-PE determined at 2.8 Å resolution, through the use of difference Fourier method and steorochemistry parameters restrained refinement with model

Structure of native laccase from Tramete
Structure of native laccase from Trametes hirsuta at 1.8 Å resolution
✍ Polyakov, Konstantin M. ;Fedorova, Tatyana V. ;Stepanova, Elena V. ;Cherkashin, 📂 Article 📅 2009 🏛 International Union of Crystallography 🌐 English ⚖ 955 KB

This paper describes the structural analysis of the native form of laccase from Trametes hirsuta at 1.8 A ˚resolution. This structure provides a basis for the elucidation of the mechanism of catalytic action of these ubiquitous proteins. The 1.8 A resolution native structure provided a good level of