X-Ray Crystallographic Analysis of Pokeweed Antiviral Protein-II after Reductive Methylation of Lysine Residues

2000 ◽  
Vol 275 (2) ◽  
pp. 549-552 ◽  
Author(s):  
I.V. Kurinov ◽  
C. Mao ◽  
J.D. Irvin ◽  
F.M. Uckun
Keyword(s):  
Crystallographic Analysis ◽  
Pokeweed Antiviral Protein ◽  
Antiviral Protein ◽  
Reductive Methylation ◽  
X Ray ◽  
Lysine Residues ◽  
Pokeweed Antiviral Protein Ii

Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues

1999 ◽  
Vol 55 (4) ◽  
pp. 931-933 ◽  
Author(s):  
Masanori Kobayashi ◽  
Michio Kubota ◽  
Yoshiki Matsuura
Keyword(s):  
Crystal Quality ◽  
X Ray Diffraction ◽  
Reductive Methylation ◽  
Orthorhombic Space Group ◽  
Trehalose Synthase ◽  
X Ray ◽  
Cell Parameters ◽  
Lysine Residues ◽  
Trehalose Biosynthesis ◽  
Enzyme Molecules

Maltooligosyl trehalose synthase, one of the two enzymes in the coupled trehalose biosynthesis system in Sulfolobus acidocaldarius, has been purified and crystallized. The chemical modification of this enzyme by reductive methylation of lysine residues significantly improved the crystal quality for X-ray diffraction experiments. The crystals of the modified enzyme belong to orthorhombic space group P212121, with unit-cell parameters a = 56.70, b = 140.1, c = 205.2 Å measured at cryo-temperature, and are found to contain two enzyme molecules per asymmetric unit.

Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein

1992 ◽  
Vol 226 (1) ◽  
pp. 281-283 ◽  
Author(s):  
Masashi Miyano ◽  
Krzystof Appelt ◽  
Masatoshi Arita ◽  
Noriyuki Habuka ◽  
Jiro Kataoka ◽  
...  
Keyword(s):  
Crystallographic Analysis ◽  
Antiviral Protein ◽  
X Ray ◽  
Mirabilis Antiviral Protein

scholarly journals Full-length nisin immunity protein NisI fromLactococcus lactisin a lipid-free form: crystallization and X-ray analysis

2017 ◽  
Vol 73 (7) ◽  
pp. 404-408 ◽  
Author(s):  
Jin Hee Jeong ◽  
Sung Chul Ha
Keyword(s):  
Full Length ◽  
Free Form ◽  
Reductive Methylation ◽  
Immunity Protein ◽  
X Ray ◽  
Cell Parameters ◽  
Peg 4000 ◽  
Lysine Residues ◽  
Lactobacillus Lactis ◽  
Self Protection

NisI is a lantibiotic-binding lipoprotein that is specific for nisin. Nisin-producing microorganisms use NisI as an immunity protein for self-protection against nisin. Here, the purification, crystallization and preliminary X-ray diffraction of full-length NisI fromLactobacillus lactisin a lipid-free form (NisI22-C) are reported. Importantly, reductive methylation of the lysine residues in NisI22-Cwas essential for initial crystallization. Only methylated NisI22-Ccrystallized. The optimized crystals of methylated NisI22-Cwere grown in 30–40 mMammonium sulfate, 0.1 Msodium acetate pH 4.6, 16–18% PEG 4000 at 295 K and diffracted to 1.9 Å resolution. The crystal belonged to space groupP212121, with unit-cell parametersa= 45.99,b= 76.67,c= 76.39 Å, α = β = γ = 90.0°. Assuming the presence of one molecule in the asymmetric unit, the estimated Matthews coefficient (VM) is 2.58 Å3 Da−1and the estimated solvent content is 52.3%.

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

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