Structural differences in solution and crystalline forms of metmyoglobin

Autor:	G. Bunker, Ayene I, Stern Ea, Ke Zhang, K. S. Reddy, Britton Chance
Rok vydání:	1991
Předmět:	Male Diffraction Spectrum Analysis X-Rays Whales Crystal structure Spermatozoa Biochemistry Solutions chemistry.chemical_compound Crystallography Myoglobin chemistry Atomic resolution Atom X-ray crystallography Animals Local environment Absorption (chemistry) Crystallization Metmyoglobin
Zdroj:	Biochemistry. 30:9116-9120
ISSN:	1520-4995 0006-2960
DOI:	10.1021/bi00101a030
Popis:	For several decades X-ray diffraction studies have been the paragon of biological structure studies at atomic resolution. Diffraction provides three-dimensional structure information, which is essential to our fundamental understanding of protein function. However, since X-ray diffraction cannot be done to atomic resolution on proteins in their native solution or membrane-bound state, the possibility exists that the conformations of the protein in crystals are slightly different from the conformations in solution, and attempts to interpret details of the structure may be misleading and without physiological relevance. In this paper, we show that this concern is justified for a familiar protein, myoglobin. Performing X-ray absorption fine structure experiments on both solution and crystalline met-myoglobin (met-Mb), we find significant differences in the local environment of the iron between the two states. Specifically, the average iron-nearest neighbor atom distance in the crystalline form is 0.05 A shorter than that in the solution form, and the iron-nearest neighbor bond is more rigid in the crystalline met-Mb. Possible artifactual explanations for the differences have been ruled out.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cea2303c355c313881f7dcd51342b7ca https://doi.org/10.1021/bi00101a030 Zobrazit plný text záznamu