5lym
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STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS
OverviewOverview
Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown, at low pH in the presence of NaNO(3) belong to space group P2(1) with, unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8, degrees with two molecules in the asymmetric unit. 1.8 A resolution, intensity data, collected on a CAD-4 diffractometer, contained 17 524, reflections with F > 3sigma (93% complete). Our earlier preliminary 1.8 A, model was refitted and refined using X-PLOR to an R value of 0.189. The, deviations in the model from ideal geometry are 0.013 A in bond lengths, and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms, between the two molecules is 0.42 A. A comparison of HEL in different, polymorphic crystal forms reveals that the prominent structural, variability among them resides in two exposed regions 45-50 and 65-73, which are also regions of lattice contacts.
About this StructureAbout this Structure
5LYM is a Single protein structure of sequence from Gallus gallus with NO3 as ligand. This structure superseeds the now removed PDB entry 1LYM. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Studies of monoclinic hen egg-white lysozyme. IV. X-ray refinement at 1.8 A resolution and a comparison of the variable regions in the polymorphic forms., Rao ST, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):170-5. PMID:15299739
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