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Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase.
J Struct Biol. 1998 Jan; 121(1):73-5.JS

Abstract

A fully active 83-kDa truncated form of recombinant hyaluronate lyase from Streptococcus pneumoniae was crystallized by the hanging drop vapor diffusion method using ammonium sulfate as a precipitating agent. Crystals grew at room temperature using a variety of buffers with pH around 6. The crystals diffract X-rays beyond 2.0 A resolution using Cu K alpha radiation and a rotating-anode X-ray source. They belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 84.2, b = 104.2, c = 104.6 A, and alpha = beta = gamma = 90.0 degrees. The VM value of 2.9 A3/Da is consistent with only one molecule of the enzyme in the asymmetric unit and the solvent content of 57%. Diffraction data 94.7% complete to 2.0 A resolution with Rsym of 5.4% were collected from one native crystal at room temperature. The search for heavy-atom derivatives to solve the structure is in progress.

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Authors+Show Affiliations

Jedrzejas MJ
Department of Microbiology, University of Alabama at Birmingham 35294, USA.
Chantalat L
No affiliation info available
Mewbourne RB
No affiliation info available

MeSH

CrystallizationCrystallography, X-RayEscherichia coliMolecular WeightPeptide FragmentsPolysaccharide-LyasesRecombinant ProteinsStreptococcus pneumoniae

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9573623

Citation

Jedrzejas, M J., et al. "Crystallization and Preliminary X-ray Analysis of Streptococcus Pneumoniae Hyaluronate Lyase." Journal of Structural Biology, vol. 121, no. 1, 1998, pp. 73-5.
Jedrzejas MJ, Chantalat L, Mewbourne RB. Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase. J Struct Biol. 1998;121(1):73-5.
Jedrzejas, M. J., Chantalat, L., & Mewbourne, R. B. (1998). Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase. Journal of Structural Biology, 121(1), 73-5.
Jedrzejas MJ, Chantalat L, Mewbourne RB. Crystallization and Preliminary X-ray Analysis of Streptococcus Pneumoniae Hyaluronate Lyase. J Struct Biol. 1998;121(1):73-5. PubMed PMID: 9573623.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase. AU - Jedrzejas,M J, AU - Chantalat,L, AU - Mewbourne,R B, PY - 1998/5/9/pubmed PY - 1998/5/9/medline PY - 1998/5/9/entrez SP - 73 EP - 5 JF - Journal of structural biology JO - J Struct Biol VL - 121 IS - 1 N2 - A fully active 83-kDa truncated form of recombinant hyaluronate lyase from Streptococcus pneumoniae was crystallized by the hanging drop vapor diffusion method using ammonium sulfate as a precipitating agent. Crystals grew at room temperature using a variety of buffers with pH around 6. The crystals diffract X-rays beyond 2.0 A resolution using Cu K alpha radiation and a rotating-anode X-ray source. They belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 84.2, b = 104.2, c = 104.6 A, and alpha = beta = gamma = 90.0 degrees. The VM value of 2.9 A3/Da is consistent with only one molecule of the enzyme in the asymmetric unit and the solvent content of 57%. Diffraction data 94.7% complete to 2.0 A resolution with Rsym of 5.4% were collected from one native crystal at room temperature. The search for heavy-atom derivatives to solve the structure is in progress. SN - 1047-8477 UR - https://www.unboundmedicine.com/medline/citation/9573623/Crystallization_and_preliminary_X_ray_analysis_of_Streptococcus_pneumoniae_hyaluronate_lyase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1047-8477(98)93963-6 DB - PRIME DP - Unbound Medicine ER -