Structure Of Lysozyme: A Fourier Map of the Electron Density at 6 Å Resolution obtained by X-ray Diffraction

Blake, C. C. F.; Fenn, R. H.; North, A. C. T.; Phillips, David; Poljak, Roberto J.

doi:10.1038/1961173a0

Cited by 96 publications

(34 citation statements)

References 18 publications

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“…In several cases there is now crystallographic information about the similar conformations of closely related molecules, or of identical molecules under slightly different conditions: met-myoglobin and the subunits of oxy and deoxyhaemoglobin (18,43,44); different crystal forms of lysozyme (45,46) ; ribonuclease A and ribonuclease S (7,47); the different autolysis products of chymotrypsin (48,49,129) ; molecules of a-chymotrypsin in dif ferent environments in the same crystal (5). Even stronger evidence that proteins have a definite, equilibrium conformation which is reached without intervention of any special agency comes from experiments on renaturation of ribonuclease and other proteins (SO-52) and the total syntheses of ribo nuclease reported recently (53,54).…”

Section: The Folding Of Protein Moleculesmentioning

confidence: 99%

X-Ray Diffraction Studies of Enzymes

Blow¹,

Steitz²

1970

Annu. Rev. Biochem.

200

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Section: The Folding Of Protein Moleculesmentioning

confidence: 99%

X-Ray Diffraction Studies of Enzymes

Blow¹,

Steitz²

1970

Annu. Rev. Biochem.

200

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“…The first X-ray structure determination of hen egg-white lysozyme (HEWL) was a tetragonal form of the enzyme (Blake, Fenn, North, Phillips & Poljak, 1962;Blake et al, 1965;Phillips, 1966Phillips, , 1967. Then, the structures of triclinic, monoclinic and orthorhombic crystal forms have been determined at different resolutions and under various conditions of temperature and pressure (Table 1).…”

Section: Introductionmentioning

confidence: 99%

High-Resolution Structure (1.33 Å) of a HEW Lysozyme Tetragonal Crystal Grown in the APCF Apparatus. Data and Structural Comparison with a Crystal Grown under Microgravity from SpaceHab-01 Mission

Vaney¹,

Maignan²,

Riès-Kautt³

et al. 1996

Acta Crystallogr D Biol Crystallogr

295

264

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Crystals of tetragonal hen egg-white lysozyme were grown using Advanced Protein Crystallization Facility (APCF) apparatus under a microgravity environment (SpaceHab-01 mission) and ground control conditions. Crystals were grown from NaCI as a crystallizing agent at pH 4.3. The X-ray diffraction patterns of the best diffracting ground-and space-grown crystals were recorded using synchrotron radiation and an image plate on the W32 beamline at LURE. Both ground-and space-grown crystals showed nearly equivalent maximum resolution of 1.3-1.4,~. Refinements were carried out with the program X-PLOR with final R values of 18.45 and 18.27% for structures from ground-and spacegrown crystals, respectively. The two structures are nearly identical with the root-mean-square difference on all protein atoms being 0.13/~. Some residues of the two refined structures show multiple alternative conformations. Two ions were localized into the electron-density maps of the two structures: one chloride ion at the interface between two symmetry-related molecules and one sodium ion stabilizing the loop Ser60-Leu75. The sodium ion is surrounded by six ligands which form a bipyramid around it at distances of 2.2-2.6 A,.

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“…In a previous paper [ 11, we pointed out the effect of temperature on the crystallization of hen egg-white lysozyme (EC 3.2.1.17), which enabled us to characterize a new orthorhombic form, called B form, quite different from the tetragonal crystals (A form) [2,3]. The present note deals with our first results on the influence of urea.…”

Section: Introductionmentioning

confidence: 80%