X-ray crystallography provides structural details of biological macromolecules. Whereas routine data are collected close to 100β K in order to mitigate radiation damage, more exotic temperature-controlled experiments in a broader temperature range from 15β K to room temperature can provide both dynami
New trends in macromolecular X-ray crystallography
β Scribed by Jean-Pierre Wery; Richard W Schevitz
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 605 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
β¦ Synopsis
Advances in experimental and computational techniques have reaffirmed the role of protein X-ray crystallography as one of the primary providers of structural information both to enhance our fundamental understanding of biological systems and also to assist the design and optimization of important therapeutics. Today, the most important challenge facing macromolecular X-ray crystallography is the need to grow suitable crystals of a given protein. Once this has been accomplished, most often the question is not whether the structure will be solved but rather how fast this will be done. A dramatic example of this is the crystal structure of cytochrome c oxidase. The search for crystallization conditions took about 15 years and then the structure was solved in about one year.
π SIMILAR VOLUMES
An indicator which is calculated after the data reduction of aΒ test data set may be used to estimate the (systematic) instrument error at a macromolecular X-ray source. The numerical value of the indicator is the highest signal-to-noise [__I__/Ο(__I__)] value that the experimental setup can produce
Radiation damage in macromolecular crystals is not suppressed even at 90 K. This is particularly true for covalent bonds involving an anomalous scatterer (such as bromine) at the 'peak wavelength'. It is shown that a series of absorption spectra recorded on a brominated RNA faithfully monitor the ex
23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A Λ(6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the p