7LVC

E. coli DHFR by Native Mn,P,S-SAD at Room Temperature

7LVC の概要

• エントリーDOI: 10.2210/pdb7lvc/pdb
• 関連するPDBエントリー: 7L84
• 分子名称: Dihydrofolate reductase, FOLIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: dihydrofolate reductase, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19510.83

構造登録者

Greisman, J.B.,Dalton, K.M.,Hekstra, D.R. (登録日: 2021-02-24, 公開日: 2021-03-17, 最終更新日: 2024-11-13)

主引用文献

Greisman, J.B.,Dalton, K.M.,Sheehan, C.J.,Klureza, M.A.,Kurinov, I.,Hekstra, D.R.
Native SAD phasing at room temperature.
Acta Crystallogr D Struct Biol, 78:986-996, 2022

PubMed Abstract: Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature.

PubMed: 35916223
DOI: 10.1107/S2059798322006799

実験手法

X-RAY DIFFRACTION (1.7 Å)