5LYM

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

Replaces:  1LYM

Summary for 5LYM

• Entry DOI: 10.2210/pdb5lym/pdb
• Descriptor: LYSOZYME, NITRATE ION (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 2
• Total formula weight: 29034.35

Authors

Rao, S.T.,Sundaralingam, M. (deposition date: 1995-07-20, release date: 1995-10-15, Last modification date: 2024-06-05)

Primary citation

Rao, S.T.,Sundaralingam, M.
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.
Acta Crystallogr.,Sect.D, 52:170-175, 1996

PubMed Abstract: 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.

PubMed: 15299739
DOI: 10.1107/S0907444995009504

Experimental method

X-RAY DIFFRACTION (1.8 Å)