An X-ray investigation of lysozyme iodide and nitrate

King, G. S. D.

doi:10.1107/s0365110x59000603

Cited by 11 publications

(5 citation statements)

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“…The cell parameters of the two forms are: type I" space group P2~, a = 27.62, b = 63.56, e = 60.51 A, fl = 90.06 ° , type II: space group P2 l, a = 28.12, b = 63.61, ¢ = 60.52A, fl = 91.05 °. These parameters are in satisfactory agreement with those previously reported by Crick (1953), King (1959) and Steinrauf (1959).…”

Section: Structure Determinations (A) the Monoclinie Formsupporting

confidence: 93%

“…is odd, and this tendency is more marked in the type I crystals. As suggested by Crick (1953) and King (1959) Direct methods of phase determination were applied to the analysis of that derivative, using MULTAN (Germain, Main & Woolfson, 1971) as described by Wilson (1978). The isomorphous differences were normalized, and the 172 terms with E values greater than unity were selected as input.…”

Section: Structure Determinations (A) the Monoclinie Formmentioning

confidence: 99%

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The structures of the monoclinic and orthorhombic forms of hen egg-white lysozyme at 6 Å resolution

Artymiuk¹,

Blake²,

Rice³

et al. 1982

Acta Crystallogr B Struct Crystallogr Cryst Chem

151

132

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The structures of a monoclinic and an orthorhombic form of hen egg-white lysozyme (HEWL) have been determined at 6A resolution by the method of isomorphous replacement. At this resolution the conformations of the molecules are indistinguishable from that of the tetragonal form of HEWL. The two molecules in the asymmetric unit of the monoclinic form are related by a translation of approximately (a/2 + c/2). The tight packing of the molecules in the unit cell prevents substrate-binding studies being carried out on this crystal form. In the orthorhombic crystals the sugar-binding sites A and B are blocked but the lower part of the active-site cleft appears to be accessible. Thus, neither of these crystal forms is ideally suited to the binding of true substrate at sub-zero temperatures.

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Section: Structure Determinations (A) the Monoclinie Formsupporting

confidence: 93%

Section: Structure Determinations (A) the Monoclinie Formmentioning

confidence: 99%

The structures of the monoclinic and orthorhombic forms of hen egg-white lysozyme at 6 Å resolution

Artymiuk¹,

Blake²,

Rice³

et al. 1982

Acta Crystallogr B Struct Crystallogr Cryst Chem

151

132

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“…The five anions found in this study are clearly not the only ones present in tetragonal lysozyme crystals. Earlier investigations using physico-chemical methods found many morc anions (Palmer et al, 1948;Carr, 1953;King, 1959). The remaining ions are either bound to the crystalline protein or free within the solvent channels.…”

Section: Discussionmentioning

confidence: 99%

“…In other physico-chemical (i.e. non-crystallographic) binding studies the number of anions found includes those present in the solvent channels, making it impossible to determine those rigidly bound only to the crystalline matrix (Palmer et al, 1948: Carr, 1953King, 1959). However, these studies do suggest that there may be more anion-binding sites in tetragonal lysozyme than the single site found by Phillips and co-workers.…”

Section: Introductionmentioning

confidence: 95%

“…The importance of anions in the crystallization of lysozyme is known from their effect on the crystal solubility and the crystal form. Early investigations showed that tetragonal crystals were produced when chloride and bromide salts were employed as precipitants, whilst iodide and thiocyanate salts produced monoclinic crystals and nitrate salts gave monoclinic or triclinic crystals (Alderton & Fevoid, 1946;Steinrauf, 1959;King, 1959). Crystal solubilities showed a similar trend with thiocyanate ions causing the crystals to be least soluble and chloride ions causing them to be more soluble (Ri6s-Kautt & Ducruix, 1989;Pusey & Munson, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Locations of Bromide Ions in Tetragonal Lysozyme Crystals

Lim

Nadarajah

Forsythe

et al. 1998

Acta Crystallogr D Biol Crystallogr

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Anions have been shown to play a dominant role in the crystallization of chicken egg-white lysozyme from salt solutions. Previous studies employing X-ray crystallography have found one chloride ion binding site in the tetragonal crystal form of the protein and four nitrate ion binding sites in the monoclinic form. In this study the anion positions in the tetragonal form were determined from the difference Fourier map obtained from lysozyme crystals grown in bromide and chloride solutions. Five possible anion-binding sites were found in this manner. Some of these sites were in pockets containing basic residues while others were near neutral, but polar, residues. The sole chloride ion binding site found in previous studies was confirmed, while four further sites were found which corresponded to the four binding sites found for nitrate ions in monoclinic crystals. The study suggests that most of the anion-binding sites in lysozyme remain unchanged even when different anions and different crystal forms of lysozyme are employed.

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Neuere Untersuchungen an Lysozymen

Jollès¹

1964

Angewandte Chemie

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An X-ray investigation of lysozyme iodide and nitrate

Cited by 11 publications

References 0 publications

The structures of the monoclinic and orthorhombic forms of hen egg-white lysozyme at 6 Å resolution

The structures of the monoclinic and orthorhombic forms of hen egg-white lysozyme at 6 Å resolution

Locations of Bromide Ions in Tetragonal Lysozyme Crystals

Neuere Untersuchungen an Lysozymen

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