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7L52

Crystal Structure of the Metallo Beta Lactamase L1 from Stenotrophomonas maltophilia Determined by Serial Crystallography

7L52 の概要
エントリーDOI10.2210/pdb7l52/pdb
関連するPDBエントリー6UA1
分子名称Putative metallo-beta-lactamase l1 (Beta-lactamase type ii) (Ec 3.5.2.6) (Penicillinase), ZINC ION (3 entities in total)
機能のキーワードmetallo beta lactamase, serial crystallography, structural genomics, center for structural genomics of infectious diseases, hydrolase, csgid
由来する生物種Stenotrophomonas maltophilia (strain K279a)
タンパク質・核酸の鎖数1
化学式量合計29374.76
構造登録者
主引用文献Sherrell, D.A.,Lavens, A.,Wilamowski, M.,Kim, Y.,Chard, R.,Lazarski, K.,Rosenbaum, G.,Vescovi, R.,Johnson, J.L.,Akins, C.,Chang, C.,Michalska, K.,Babnigg, G.,Foster, I.,Joachimiak, A.
Fixed-target serial crystallography at the Structural Biology Center.
J.Synchrotron Radiat., 29:1141-1151, 2022
Cited by
PubMed Abstract: Serial synchrotron crystallography enables the study of protein structures under physiological temperature and reduced radiation damage by collection of data from thousands of crystals. The Structural Biology Center at Sector 19 of the Advanced Photon Source has implemented a fixed-target approach with a new 3D-printed mesh-holder optimized for sample handling. The holder immobilizes a crystal suspension or droplet emulsion on a nylon mesh, trapping and sealing a near-monolayer of crystals in its mother liquor between two thin Mylar films. Data can be rapidly collected in scan mode and analyzed in near real-time using piezoelectric linear stages assembled in an XYZ arrangement, controlled with a graphical user interface and analyzed using a high-performance computing pipeline. Here, the system was applied to two β-lactamases: a class D serine β-lactamase from Chitinophaga pinensis DSM 2588 and L1 metallo-β-lactamase from Stenotrophomonas maltophilia K279a.
PubMed: 36073872
DOI: 10.1107/S1600577522007895
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.85 Å)
構造検証レポート
Validation report summary of 7l52
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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