ISDA: 7L52

Deposition Date 2020-12-21

Release Date 2020-12-30

Last Version Date 2026-03-25

Entry Detail

PDB ID:

7L52

Keywords:

HYDROLASE

Title:

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

Biological Source:

Source Organism(s):

Stenotrophomonas maltophilia (strain K279a) (Taxon ID: 522373)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.85 Å

R-Value Free:

0.21

R-Value Work:

0.17

R-Value Observed:

0.17

Space Group:

P 64 2 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Putative metallo-beta-lactama
Gene (Uniprot):Smlt2667
Chain IDs:A
Chain Length:275
Number of Molecules:1
Biological Source:Stenotrophomonas maltophilia (strain K279a)

UniProt ID:B2FTM1 Pfam ID:PF00753 EC:3.5.2.6

Ligand Molecules

Primary Citation

Fixed-target serial crystallography at the Structural Biology Center.

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.Show

J Synchrotron Radiat 29 1141 1151 (2022)

PMID: 36073872 DOI: 10.1107/S1600577522007895

Abstact

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 beta-lactamases: a class D serine beta-lactamase from Chitinophaga pinensis DSM 2588 and L1 metallo-beta-lactamase from Stenotrophomonas maltophilia K279a.

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Protein

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Primary Citation of related structures

Abstact

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