Cryocrystallography of metalloprotein reaction intermediates

Carrie M. Wilmot, Arwen R. Pearson

Research output: Contribution to journalReview articlepeer-review

18 Scopus citations


Freeze-trapping reaction intermediates in macromolecular crystals is now a proven technique for obtaining their high-resolution structures by X-ray crystallography. The structural study of metalloprotein mechanisms has spearheaded this work, mainly because of the increased availability of single-crystal UV/visible spectrophotometry that enables reaction monitoring in the crystalline state. In particular, through formation of the frozen glass state, the stabilization of intermediates involving dissolved gases has yielded some of the most spectacular results. Metalloprotein systems still dominate this field, and the most recent successes, along with the accompanying advances in methodology, are presented.

Original languageEnglish (US)
Pages (from-to)202-207
Number of pages6
JournalCurrent opinion in chemical biology
Issue number2
StatePublished - Apr 1 2002


Dive into the research topics of 'Cryocrystallography of metalloprotein reaction intermediates'. Together they form a unique fingerprint.

Cite this